PROCESSING MECHANISMS IN THE BIOSYNTHESIS OF PROTEINS*
1980; Wiley; Volume: 343; Issue: 1 Linguagem: Inglês
10.1111/j.1749-6632.1980.tb47238.x
ISSN1749-6632
AutoresDonald F. Steiner, Paul Quinn, Shu Jin Chan, Jon W. Marsh, Howard S. Tager,
Tópico(s)Glycosylation and Glycoproteins Research
ResumoAnnals of the New York Academy of SciencesVolume 343, Issue 1 p. 1-16 PROCESSING MECHANISMS IN THE BIOSYNTHESIS OF PROTEINS* Donald F. Steiner, Donald F. Steiner Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this authorPaul S. Quinn, Paul S. Quinn Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this authorShu Jin Chan, Shu Jin Chan Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this authorJon Marsh, Jon Marsh Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this authorHoward S. Tager, Howard S. Tager Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this author Donald F. Steiner, Donald F. Steiner Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this authorPaul S. Quinn, Paul S. Quinn Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this authorShu Jin Chan, Shu Jin Chan Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this authorJon Marsh, Jon Marsh Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this authorHoward S. Tager, Howard S. Tager Department of Biochemistry University of Chicago Chicago, Illinois 60637Search for more papers by this author First published: May 1980 https://doi.org/10.1111/j.1749-6632.1980.tb47238.xCitations: 330 * Work from this Laboratory has been supported by Grants AM 13914, AM 20S9S, and AM 17046 of the United States Public Health Service and by grants-in-aid from the Lolly Coustan Memorial Fund, the Kroc Foundation, and the Novo Research Laboratories. AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat References 1 Steiner, D.F., W. Kemmler, H.S. Taoer & J.D. Peterson. 1974. Proteolytic processing in the biosynthesis of insulin and other proteins. Fed. Proc. 33: 2105–2115. CASPubMedWeb of Science®Google Scholar 2 Steiner, D.F. & J.L. Clark 1968. The spontaneous reoxidation of reduced beef and rat proinsulins. Proc. Nat. Acad. Sci. USA 60: 622–629. 10.1073/pnas.60.2.622 CASPubMedWeb of Science®Google Scholar 3 Patzelt, C., S.J. Chan, J. Duguid, G. Hortin, P. Keim, R.L. Heinrikson & D.F. Steiner. 1978. Biosynthesis of polypeptide hormones in intact and cell-free systems. In Regulatory Proteolytic Enzymes and Their Inhibitors. Proc. Vol. 47, Symp. A6. S. Magnusson et al., Eds.: 69–78. Pergamon Press. New York . 10.1016/B978-0-08-022628-6.50009-9 Google Scholar 4 Steiner, D.F. 1978. On the role of the proinsulin C-peptide. Diabetes 27(Suppl. 1): 145–148. 10.2337/diab.27.1.S145 CASPubMedWeb of Science®Google Scholar 5 Steiner, D.F., W. Kemmler, J.L. Clark, P.E. Over & A.M. Rubenstein. 1972. The biosynthesis of insulin. In Handbook of Physiology–-Endocrinology I. D.F. Steiner & N. Freinkel, Eds.: 175–198. Williams and Wilkins. Baltimore . Google Scholar 6 Mains, R. E. & B.A. Eipper. 1976. Biosynthesis of adrenocorticotropic hormone in mouse pituitary cells. J. Biol. Chem. 251: 4115–4120. CASPubMedWeb of Science®Google Scholar 7 Mains, R.E., B.A. Eipper & N. Lino. 1977. Common precursors to corticotrophins and endorphins. Proc. Nat. Acad. Sci. USA 74: 3014–3018. 10.1073/pnas.74.7.3014 CASPubMedWeb of Science®Google Scholar 8 Korant, B.D. 1975. Regulation of animal virus replication by protein cleavage. In Proteases and Biological Control. E. Reich, D.B. Ripkin & E. Shaw, Eds.: 621–644. Cold Spring Harbor Laboratory. Google Scholar 9 Poyton, R.O. & E. McKemmie. 1979. A polyprotein precursor to all four cytoplasmically-translated subunits of cytochrome c oxidase from Saccharomyces cervisiae. J. Biol. Chem.. 254. In press. PubMedGoogle Scholar 10 Poyton, R. O. & E. McKemmie. 1979. Post-translational processing and transport of the polyprotein precursor to subunits IV-VII of yeast cytochrome c oxidase. J. Biol. Chem.. 254. In press. PubMedGoogle Scholar 11 Blobel, G. & B. Dobberstein. 1975. Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane bound ribosomes of murine myeloma. J. Cell Biol. 67: 835–851. 10.1083/jcb.67.3.835 CASPubMedWeb of Science®Google Scholar 12 Blobel, G. & B. Dobberstein. 1975. Transfer of proteins across membranes. II. Reconstitution of functional rough microsomes from heterologous components. J. Cell Biol. 67: 852–862. 10.1083/jcb.67.3.852 CASPubMedWeb of Science®Google Scholar 13 Strauss, A.W., C.A. Bennett, A.M. Donohue, J.A. Rodkey, I. Boime & A.W. Alberts. 1978. Conversion of rat pre-proalbumin to proalbumin in vitro by ascites membranes. Demonstration by NH2-terminal sequence analysis. J. Biol. Chem. 253: 6270–6274. CASPubMedWeb of Science®Google Scholar 14 Dorner, A.J. & B. Kemper. 1978. Conversion of pre-proparathyroid hormone to proparathyroid hormone by dog pancreatic microsomes. Biochemistry 17: 5550–5555. 10.1021/bi00618a034 CASPubMedWeb of Science®Google Scholar 15 Shields, D. & G. Blobel. 1978. Efficient cleavage and segregation of nascent presecretory proteins in a reticulocyte lysate supplemented with microsomal membranes. J. Biol. Chem. 253: 3753–3756. CASPubMedWeb of Science®Google Scholar 16 Jackson R.C. & G. Blobel. 1977. Post-translational cleavage of presecretory proteins with an extract of rough microsomes from dog pancreas containing signal peptidase activity. Proc. Nat. Acad. Sci. USA 74: 5598–5602. 10.1073/pnas.74.12.5598 CASPubMedWeb of Science®Google Scholar 17 Katz F. N., J.E. Rothman, V.R. Linoappa, G Blobel & H.F Lodish. 1977. Membrane assembly in vitro: synthesis, glycosylation, and asymmetric insertion of a transmembrane protein. Proc. Nat. Acad. Sci. USA 74: 3278–3282. 10.1073/pnas.74.8.3278 CASPubMedWeb of Science®Google Scholar 18 Kreibich G., R. Grenbenau, W. Mok, B. Pereyra, E. Rodiriouez-Boulan, B Ulrich & D.D. Sabatini. 1977. Two membrane proteins of rat liver microsomes related to ribosome binding. Fed. Proc. 36: 656. Web of Science®Google Scholar 19 Duouid J.R., C. Patzelt, S.J. Chan, A. Labrecque, R. Hastings, P. Quinn & D.F. Steiner. 1978. New aspects of insulin biosynthesis. Presented at the International Symposium on Proinsulin, Insulin, and C-Peptide. Tokushima, Japan, July, 1978. In press. Google Scholar 20 Chan S.J., C. Patzelt, J. Duguid, P. Quinn, A. Labrecque, B. Noyes, P. Keim, R. L. Heinrikson & D.F. Steiner. 1979. Precursors in the biosynthesis of insulin and other peptide hormones. In 11th Miami Winter Symp., Vol. 16. Academic Press. New York . Google Scholar 21 Chou P.Y. & G.D. Fasman. 1978. Prediction of protein conformation. Ann. Rev. Biochem. 47: 251. 10.1146/annurev.bi.47.070178.001343 CASPubMedWeb of Science®Google Scholar 22 Steiner D.F., P.S. Quinn, C. Patzelt, S.J. Chan, J. Marsh & H.S. Taoer. 1979. Limited proteolytic cleavage in the biosynthesis of proteins. In Cell Biology: A Comprehensive Treatise. L. Goldstein & D.M. Prescott, Eds. Vol. IV. Academic Press. New York . In press. Google Scholar 23 Lin J.J.C., H. Kanazawa, J. Ozols & H.C. Wu. 1978. An Escherichia coli mutant with an amino acid alteration within the signal sequence of outer membrane prolipoprotein. Proc. Nat. Acad. Sci. USA 75: 4891–4895. 10.1073/pnas.75.10.4891 CASPubMedWeb of Science®Google Scholar 24 Dirienzo J.M., K. Nakamura & M. Inouye. 1978. The outer membrane proteins of gram-negative bacteria: biosynthesis, assembly and functions. Ann. Rev. Biochem. 47: 481–532. 10.1146/annurev.bi.47.070178.002405 CASPubMedWeb of Science®Google Scholar 25 Burstein Y. & I. Schechter. 1978. Primary structures of n-terminal extra peptide segments linked to the variable and constant regions of immunoglobulin light chain precursors: implications on the organizations and controlled expression of immunoglobulin genes. Biochemistry 17: 2392–2400. 10.1021/bi00605a022 CASPubMedWeb of Science®Google Scholar 26 Palmiter R.D., J. Gaonon & K.A. Walsh. 1978. Ovalbumin: A secrected protein without a transient hydrophobic leader sequence. Proc. Nat. Acad. Sci. USA 75: 94–98. 10.1073/pnas.75.1.94 CASPubMedWeb of Science®Google Scholar 27 Lingappa, V.R., J.R. Lingappa & G. Blobel. 1979. Chicken ovalbumin contains an internal signal sequence. Nature 281: 117–121. 10.1038/281117a0 CASPubMedWeb of Science®Google Scholar 28 Patzelt C., A.D. Labrecque, J.R. Duguid, R.J. Carroll, P. Keim, R.L. Heinrikson & D.F. Steiner. 1978. Detection and kinetic behavior of preproinsulin in pancreatic islets. Proc. Nat. Acad. Sci. USA 75: 1260–1264. 10.1073/pnas.75.3.1260 CASPubMedWeb of Science®Google Scholar 29 Inouye H. & J. Beckwith. 1977. Synthesis and processing of an E. coll alkaline phosphatase precursor in vitro. Proc. Nat. Acad. Sci. USA 74: 1440–1444. 10.1073/pnas.74.4.1440 CASPubMedWeb of Science®Google Scholar 30 Inouye, M. & S. Halegoua. 1979. Secretion and membrane localization of proteins in E. coli. Chemical Rubber Co. Reviews. In press. Google Scholar 31 Smith, W.P., P.-C. Tai & B.D. Davis. 1978. Nascent peptide as sole attachment of polysomes to membranes in bacteria. Proc. Nat. Acad. Sci. USA 75: 814–817. 10.1073/pnas.75.2.814 CASPubMedWeb of Science®Google Scholar 32 Gibson, R., S. Schlesinoer & S. Kornfield. 1979. The nonglycosylated glycoprotein of vesicular stomatitis virus is temperature-sensitive and undergoes intracellular aggregation at elevated temperatures. J. Biol. Chem. 254: 3600–3607. CASPubMedWeb of Science®Google Scholar 33 Lingappa, V.A., F.N. Katz, H.F. Lodish & G. Blobel. 1978. A signal sequence for the insertion of a transmembrane glycoprotein. J. Biol. Chem. 253: 8667–8670. CASPubMedWeb of Science®Google Scholar 34 Lingappa, V.R., J.R. Lingappa, R. Prasad, K.E. Ebner & G. Blobel. 1978. Coupled cell-free synthesis, segregation and core glycosylation of a secretory protein. Proc. Nat. Acad. Sci. USA 75: 2338–2342. 10.1073/pnas.75.5.2338 CASPubMedWeb of Science®Google Scholar 35 Jackson, R.C. & G. Blobel. 1980. Post-translational processing of full-length presecretory proteins with canine pancreatic signal peptidase. Ann. N.Y. Acad. Sci. This volume. 10.1111/j.1749-6632.1980.tb47268.x PubMedGoogle Scholar 36 Zimmerman, M., B.M. Ashe, A.W. Alberts, P.A. Pierzchala, J.C. Powers, N. Nishino, A.W. Strauss & R.A. Mumford. 1980. Protease activities present in dog pancreatic membranes that process human pre-placental lactogen. Ann. N.Y. Acad. Sci. This volume. 10.1111/j.1749-6632.1980.tb47269.x PubMedGoogle Scholar 37 Kaschnitz, R. & G. Kreil. 1978. Processing of prepromelittin by subcellular fractions from rat liver. Biochem. Biophys. Res. Commun. 83: 901–907. 10.1016/0006-291X(78)91480-8 CASPubMedWeb of Science®Google Scholar 38 Chang, C.N., G. Blobel & P. Model. 1978. Detection of prokaryotic signal peptidase in an Eschericha coli membrane fraction: Endoproteolytic cleavage of nascent fl pre-coat protein. Proc. Nat. Acad. Sci. USA 75: 361–365. 10.1073/pnas.75.1.361 CASPubMedWeb of Science®Google Scholar 39 Inouye, M., J. Dirienzo, T. Maeda, R. Thovva, K. Nakamura, N. Lee, R. Pirtle & I. Pirtle. 1980. Secretion of outer membrane proteins of Escherichia coli across the cytoplasmic membrane. Ann. N.Y. Acad. Sci. This volume. 10.1111/j.1749-6632.1980.tb47265.x PubMedGoogle Scholar 40 Strauss, A.W., M. Zimmerman, R.A. Mumford & A.W. Alberts. 1980. Processing of preproalbumin and preplacental lactogen. Ann. N.Y. Acad. Sci. This volume. 10.1111/j.1749-6632.1980.tb47250.x PubMedGoogle Scholar 41 Devillers-Thiery, A., T. Kindt, G. Scheele & G. Blobel. 1975. Homology in aminoterminal sequence of precursors to pancreatic secretory proteins. Proc. Nat. Acad. Sci. USA 72: 5016–5020. 10.1073/pnas.72.12.5016 CASPubMedWeb of Science®Google Scholar 42 Schields, D. & G. Blobel. 1977. Cell-free synthesis of fish preproinsulin and processing by heterologous mammalian microsomal membranes. Proc. Nat. Acad. Sci. USA 74: 2059–2063. 10.1073/pnas.74.5.2059 Web of Science®Google Scholar 43 Steiner, D.F., W. Kemmler, H.S. Tager, A.M. Rubenstein, Å. Lernmark & H. Zuhlke. 1975. Proteolytic mechanism in the biosynthesis of polypeptide hormones. In Proteases and Biological Control. E. Reich, D. Rifkin & E. Shaw, Eds: 531–549. Cold Spring Harbor Laboratory. Cold Spring Harbor , N.Y. . Google Scholar 44 Chretien, M., N.G. Seidah, S. Benjannet, N. Dragon, R. Routhier, T. Motomatsu, P. Crine & M. Lis. 1977. A LPH precursor model: recent develpments concerning morphine-like substances. Ann. N.Y. Acad. Sci. 297: 84–105. 10.1111/j.1749-6632.1977.tb41847.x CASPubMedGoogle Scholar 45 Roberts, J.L., M. Phillips, P.A. Rosa & E. Herbert. 1978. Steps involved in the processing of common precursor forms of adrnocorticotropin and endorphin in cultures of mouse pituitary cells. Biochemistry 17: 3609–3618. 10.1021/bi00610a030 CASPubMedWeb of Science®Google Scholar 46 Lowry, P.J., R.E. Silman, J. Hope & A.P. Scott. 1977. Structure and biosynthesis of peptides related to corticotrophins and -melanotropins. Ann. N.Y. Acad. Sci. 297: 49–60. 10.1111/j.1749-6632.1977.tb41845.x CASPubMedGoogle Scholar 47 Gregory, R. & H. Tracy. 1975. In Gastrointestinal Hormones. J. Thompson, Ed: 13–24. University of Texas Press. Austin . Google Scholar 48 Kemmler, W., J.D. Peterson & D.F. Steiner. 1971. Studies on the conversion of proinsulin to insulin. I. Conversion in vitro with trypsin and carboxypeptidase B. J. Biol. Chem. 246: 6786–6791. CASPubMedWeb of Science®Google Scholar 49 Steiner, D.F., J.L. Clark, C. Nolan, A.M. Rubenstein, E. Margoliash, F. Melani & P.E. Over. 1970. The biosynthesis of insulin and some speculations regarding the pathogenesis of human diabetes. In The Pathogenesis of Diabetes Mellitus. Proceedings of the Thirteenth Nobel Symposium. E. Cerasi and R. Luft, Eds.: 123–132. Almqvist and Wiksell. Stockholm . Google Scholar 50 Habener, J., H.T. Chang & J.T. Potts. 1977. Enzymic processing of proparathyroid hormone by cell-free extracts of parathyroid glands. Biochemestry 16: 3910–3917. 10.1021/bi00636a029 CASPubMedWeb of Science®Google Scholar 51 Eipper, B.A., R.E. Mains & D. Guenzi. 1976. High molecular weight forms of adrenocorticotropic hormone are glycoproteins. J. Biol. Chem. 251: 1421–1426. Google Scholar 52 Judah, J.D. & M.R. Nicholls. 1971. Biosynthesis of rat serum albumin. Biochem. J. 123: 649–655. 10.1042/bj1230649 CASPubMedWeb of Science®Google Scholar 53 Quinn, P.S. & J.D. Judah. 1978. Calcium-dependent Golgi-vesicle fusion and cathepsin B in the conversion of proalbumin into albumin in rat liver. Biochem. J. 172: 301–309. 10.1042/bj1720301 CASPubMedWeb of Science®Google Scholar 54 Steiner, D.F., D.D. Cunningham, L. Spigelman & B. Aten. 1967. Insulin biosynthesis: Evidence for a precursor. Science 157: 697–700. 10.1126/science.157.3789.697 CASPubMedWeb of Science®Google Scholar 55 Steiner, D.F. 1967. Evidence for a precursor in the biosynthesis of insulin. Trans. N.Y. Acad. Sci., Ser. II, 30: 60–68. 10.1111/j.2164-0947.1967.tb02452.x CASPubMedWeb of Science®Google Scholar 56 Howells, S.L. 1972. Role of ATP in the intracellular translocation of proinsulin and insulin in the rat pancreatic B cell. Nature New Biol. 235: 85–86. 10.1038/newbio235085a0 PubMedWeb of Science®Google Scholar 57 Jamieson, J.D. & G.E. Palade. 1967. Intracellular transport of secretory proteins in pancreatic exocrine cell. I. Role of peripheral elements of Golgi complex. J. Cell Biol. 34: 577–596. 10.1083/jcb.34.2.577 CASPubMedWeb of Science®Google Scholar 58 Jamieson, J.D. & G.E. Palade. 1967. Intracellular transport of secretory proteins in pancreatic exocrine cell. II. Transport to condensing vacuoles and zymogen granules. J. Cell Biol. 34: 597–615. 10.1083/jcb.34.2.597 CASPubMedWeb of Science®Google Scholar 59 Jamieson, J.D. & G.E. Palade. 1968. Intracellular transport of secretory proteins in the pancreatic exocrine wall. IV. Metabolic requirements. J. Cell Biol. 39: 589–603. 10.1083/jcb.39.3.589 CASPubMedWeb of Science®Google Scholar 60 Smith, R.E. & M.G. Farquhar. 1966. Lysosome function in the regulation of the secretory process in cells of the anterior pituitary gland. J. Cell Biol. 31: 319–347. 10.1083/jcb.31.2.319 CASPubMedWeb of Science®Google Scholar 61 Smith, R.E. & R.M. Van Frank. 1974. Substructurel localization of an enzyme in cells of rat pancreas with the ability to convert proinsulin to insulin. Endocrinology 94: A190. Google Scholar 62 Judah, J.D. & P.S. Quinn. 1978. Calcium ion-dependent vesicle fusion in the conversion of proalbumin to albumin. Nature 271: 384–385. 10.1038/271384a0 CASPubMedWeb of Science®Google Scholar 63 Kemmler, W., D.F. Steiner & J. Borg. 1973. Studies on the conversion of proinsulin to insulin. III. Studies in vitro with a crude secretion granule fraction isolated from islets of Langerhans. J. Biol. Chem. 248: 4544–4551. CASPubMedWeb of Science®Google Scholar 64 Sun, A.M., B.J. Lin & R.E. Haist. 1973. Studies on the conversion of proinsulin to insulin in the isolated islets of Langerhans in the rat. Can. J. Physiol. Pharmacol. 51: 175–182. 10.1139/y73-025 CASPubMedWeb of Science®Google Scholar 65 Grant, P.T., T.L. Coombs, N.W. Thomas & J.R. Sargent. 1971. The conversion of 14C proinsulin to insulin in isolated subcellular fractions of fish islet preparations. In Subcellular Organization and Function in Endocrine Tissues. H. Heller & K. Leder, Eds. Memoirs Soc. Endocrinology, Vol. 19: 481–495. Cambridge University Press. Google Scholar 66 Sorenson, R.L., R.D. Shank & A.W. Lindall. 1972. Effect of pH on conversion of proinsulin to insulin by a subcellular fraction of rat islets. Proc. Soc. Exp. Biol. Med. 139: 652–655. 10.3181/00379727-139-36207 CASPubMedWeb of Science®Google Scholar 67 Zühlke, H., D.F. Steiner, Å. Lernmark & C. Lipsey. 1976. Carboxypeptidase B-like and trypsin-like activities in isolated rat pancreatic islets. In Polypeptide Hormones: Molecular and Cellular Aspects. CIBA Foundation Symposium 41: 183–195. Elsevier/Excerpta Medica, North-Holland. Amsterdam . 10.1002/9780470720233.ch10 Google Scholar 68 Zuhlke, H. & D.F. Steiner Publishers. 1977. Metabolism of proinsulin and insulin in islets of Langerhans. Ergebn. Exp. Med. 28: 53–61. Google Scholar 69 Tager, H.S., S.O. Emdin, J.L. Clark & D.F. Steiner. 1973. Studies on the conversion of proinsulin to insulin. II. Evidence for a chymotrypsin-like cleavage in the connecting peptide region of insulin precursors in the rat. J. Biol. Chem. 248: 3476–3482. CASPubMedWeb of Science®Google Scholar 70 Kuzuya, H., P.M. Blix, D.L. Horwitz, A.M. Rubenstein, D.F., Steiner, O.K. Faber & C. Binder. 1978. Heterogeneity of circulating human C-peptide. Diabetes 27(Suppl. 1): 184–191. 10.2337/diab.27.1.S184 CASPubMedWeb of Science®Google Scholar 71 Butterworth, B.E. 1976. Proteolytic processing of animal virus proteins. In Current Topics in Microbiology and Immunology. Springer Verlag. New York . Google Scholar 72 Scheida, A. & P.W. Choppin. 1975. Activity of cell fusion and infectivity of proteolytic cleavage of sendai virus glycoprotein. In Proteases and Biological Control. E. Reich, D.B. Rifkin & E. Shaw, Eds. Cold Spring Harbor Conference on Cell Proliferation. Vol. 2: 645–660. Google Scholar 73 Korant, B., N. Chou, M. Lively & J. Powers. 1979. Virus-specified protease in polio-virus infected hela ceris. Proc. Nat. Acad. Sci. USA. In press. 10.1073/pnas.76.6.2992 Web of Science®Google Scholar 74 Schlesinger, M.J., M.F.G. Schmidt & G. Aliperti. 1980. Proteolytic cleavage and binding of fatty acids in the processing of Sindbis virus (SbB) and vesicular stomatitis virus (VSV) glycoproteins. Poster paper presented at the N.Y. Acad. Sci. conference on Precursor Processing in the Biosynthesis of Proteins held 2–4 May, 1979. Google Scholar 75 Highfield, P.E. & R.J. Ellis. 1978. Synthesis and transport of the small subunit of chloroplast ribulose bisphosphate carboxylase. Nature 271: 420–424. 10.1038/271420a0 CASWeb of Science®Google Scholar 76 Dobberstein, B., G. Blobel & N-H. Chua. 1977. In vitro synthesis and processing of a putative precursor for the small subunit of ribulose-1,5-bisphosphate carboxylase of Chlamydomonas reinhardtii. Proc. Nat. Acad. Sci. USA 74: 1082–1085. 10.1073/pnas.74.3.1082 CASPubMedWeb of Science®Google Scholar 77 Maccecchini, M.-L., Y. Rudin, G. Blobel & G. Schatz. 1979. Import of proteins into mitochondria: Precursor forms of the extramitochondrailly made F1-ATPase subunits in yeast. Proc. Nat. Acad. Sci. USA 76: 343–347. 10.1073/pnas.76.1.343 CASPubMedWeb of Science®Google Scholar 78 Poyton, R.O. & J. Kavanoh. 1976. Regulation of mitochondrial protein synthesis by cytoplasmic proteins. Proc. Nat. Acad. Sci. USA 73: 3947–39. 10.1073/pnas.73.11.3947 CASPubMedWeb of Science®Google Scholar 79 Haas, R. & P.C. Heinrich. 1978. The localization of an intracellular membrane-bound proteinase from rat liver. Eur. J. Biochem. 91: 171–178. 10.1111/j.1432-1033.1978.tb20949.x CASPubMedWeb of Science®Google Scholar 80 Wickner, W. 1979. The assembly of proteins into biological membranes. The membrane trigger hypothesis. Ann. Rev. Biochem. 48: In press. 10.1146/annurev.bi.48.070179.000323 CASWeb of Science®Google Scholar 81 Habener, J.F., M. Rosenblatt, B. Kemper, H.M. Kronenbero, A. Rich & J.T. Potts, Jr. 1978. Pre-proparathyroid hormone: aminoacid sequence, chemical synthesis, and some biological studies of the precursor region. Proc. Nat. Acad. Sci. USA 75: 2616–2620. 10.1073/pnas.75.6.2616 CASPubMedWeb of Science®Google Scholar 82 Chan, S.J., P. Keim & D.F. Steiner. 1976. Cell-free synthesis of rat preproinsulins: characterization and partial acid sequence determination. Proc. Nat. Acad. Sci. USA 73: 1964–1968. 10.1073/pnas.73.6.1964 CASPubMedWeb of Science®Google Scholar 83 Vllla-Komaroff, L., A. Epstratiadia, S. Broome, P. Lomedico, R. Tlzard, S.P. Naber, W.L. Chick & W. Gilbert. 1978. A bacterial clone synthesizing proinsulin. Proc. Nat. Acad. Sci. USA 75: 3727. 10.1073/pnas.75.8.3727 Web of Science®Google Scholar 84 Seeburg, P., J. Shine, J.A. Martial, J.D. Baxter, H.M. Goodman. 1977. Nucleotide sequence and amplification in bacteria of the structural gene for rat growth hormone. Nature 270: 486–494. 10.1038/270486a0 CASPubMedWeb of Science®Google Scholar 85 McKean, D.J. & R.A. Maurer. 1978. Complete amino acid sequence of the precursor region of rat protein. Biochemistry 17: 5215–5219. 10.1021/bi00617a022 CASPubMedWeb of Science®Google Scholar 86 Thibodeau, S.N., D.C. Lee & R.D. Palmiter. 1978. Identical precursors for serum transferrin and egg white conalbumin. J. Biol. Chem. 253: 3771–3774. CASPubMedWeb of Science®Google Scholar 87 Tonegawa, J., A.M. Maxam, R. Tizard, O. Bernard & W. Gilbert. 1978. Sequence of a mouse germ-line gene for a variable region of an immunoglobulin light chain. Proc. Nat. Acad. Sci. USA 75: 1485–1489. 10.1073/pnas.75.3.1485 CASPubMedWeb of Science®Google Scholar 88 Gaye, P. & J.P. Gautron. 1977. Amino sequences of the precursors of ovine caseins. Biochem. Biophys. Res. Commun. 79: 903–910. 10.1016/0006-291X(77)91196-2 CASPubMedWeb of Science®Google Scholar 89 Suchanek, G., G. Kreil & M.A. Hermondson. 1978. Amino acid sequence of honeybee prepromellitin synthesized in vitro. Proc. Nat. Acad. Sci. USA 75: 701–704. 10.1073/pnas.75.2.701 CASPubMedWeb of Science®Google Scholar 90 Sutcliffe, J.G. 1978. Nucleotide sequence of the ampicillin resistance gene of E. coli plasmid pBR322. Proc. Nat. Acad. Sci. USA 75: 3737–3741. 10.1073/pnas.75.8.3737 CASPubMedWeb of Science®Google Scholar 91 Chance, R.E., R.M. Ellis & W.W. Bromer. 1968. Porcine proinsulin: Characterization and amino acid sequence. Science 161: 165–167. 10.1126/science.161.3837.165 CASPubMedWeb of Science®Google Scholar 92 Noyes, B.E., M. Stein & K.L. Agarwal. Detection and partial sequence analysis of gastrin mRNA by using an oligodeoxynucleotide probe. Proc. Nat. Acad. Sci. USA 76: 1770–1774. Google Scholar 93 Patzelt, C., H.S. Taoer, R.C. Carroll & D.F. Steiner. 1979. Identification of proso-matostatin in pancreatic islets. Proc. Nat. Acad. Sci. USA. In press. Google Scholar 94 Taoer, H.S. & D.F. Steiner. 1973. Isolation of a glucagon-containing peptide: Primary structure of a possible fragment of proglucagon. Proc. Nat. Acad. Sci. USA 70: 2321–2325. 10.1073/pnas.70.8.2321 Web of Science®Google Scholar 95 Patzelt, C., H.S. Taoer, R.J. Carroll & D.F. Steiner. 1979. Identification and processing of proglucagon in pancreatic islets. Nature. In press. 10.1038/282260a0 PubMedWeb of Science®Google Scholar 96 Nakanishi, S., A. Inoue, T. Kita, M. Nakamura, A.C.Y. Chang, S.N. Cohen & S. Numa. 1979. Nucleotide sequence of cloned cDNA for bovine corticotropin–-lipotro-pin precursor. Nature 278: 423–427. 10.1038/278423a0 CASPubMedWeb of Science®Google Scholar 97 Kanoawa, K. & H. Matsuo. 1979. a-Neoendorphin: a "big" leuenkephalin with potent opiate activity from porcine hypothalami. Biochem. Biophys. Res. Commun. 86: 153–160. 10.1016/0006-291X(79)90394-2 PubMedWeb of Science®Google Scholar 98 Hamilton, J.W., H.D. Niall, J.W. Jacobs, H.J. Keutmann, J.T. Potts, Jr. & D.V. Cohen. 1974. Amino terminal sequence of bovine proparathyroid hormone (calcemic fraction A). Proc. Nat. Acad. Sci. USA 71: 653. 10.1073/pnas.71.3.653 CASPubMedWeb of Science®Google Scholar 99 Russell, J.H. & D.M. Geller. 1975. The structure of rat proalbumin. J. Biol. Chem. 250: 3409–3413. CASPubMedWeb of Science®Google Scholar 100 MacGregor, R.R., J.W. Hamilton, G.N. Kent, R.E. Shofstall & D.V. Cohn. 1979. The degradation of proparathormone and parathormone by parathyroid and liver Cathepsin B. J. Biol. Chem. 254: 4428–4433. CASPubMedWeb of Science®Google Scholar 101 Reich, E. Personal communication. Google Scholar 102 Yip, C.C. 1971. A bovine pancreatic enzyme catalyzing the conversion of proinsulin to insulin. Proc. Nat. Acad. Sci. USA 68: 1312–1315. 10.1073/pnas.68.6.1312 CASPubMedWeb of Science®Google Scholar 103 Ole-Moi Yoi, O., G.S. Pinkus, J. Spragg & K.F. Austen. 1979. Identification of human glandular kallikrein in the beta cell of the pancreas. New Engl. J. Med. 300: 1289–1294. 10.1056/NEJM197906073002301 Web of Science®Google Scholar Citing Literature Volume343, Issue1Precursor Processing in the Biosynthesis of ProteinsMay 1980Pages 1-16 ReferencesRelatedInformation
Referência(s)