Artigo Acesso aberto Revisado por pares

A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway.

1995; Springer Nature; Volume: 14; Issue: 11 Linguagem: Inglês

10.1002/j.1460-2075.1995.tb07241.x

ISSN

1460-2075

Autores

Patrick J. Tranel, John E. Froehlich, Abha Goyal, Kenneth Keegstra,

Tópico(s)

Plant Micronutrient Interactions and Effects

Resumo

Research Article1 June 1995free access A component of the chloroplastic protein import apparatus is targeted to the outer envelope membrane via a novel pathway. P.J. Tranel P.J. Tranel MSU-DOE-Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA. Search for more papers by this author J. Froehlich J. Froehlich MSU-DOE-Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA. Search for more papers by this author A. Goyal A. Goyal MSU-DOE-Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA. Search for more papers by this author K. Keegstra K. Keegstra MSU-DOE-Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA. Search for more papers by this author P.J. Tranel P.J. Tranel MSU-DOE-Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA. Search for more papers by this author J. Froehlich J. Froehlich MSU-DOE-Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA. Search for more papers by this author A. Goyal A. Goyal MSU-DOE-Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA. Search for more papers by this author K. Keegstra K. Keegstra MSU-DOE-Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA. Search for more papers by this author Author Information P.J. Tranel1, J. Froehlich1, A. Goyal1 and K. Keegstra1 1MSU-DOE-Plant Research Laboratory, Michigan State University, East Lansing 48824-1312, USA. The EMBO Journal (1995)14:2436-2446https://doi.org/10.1002/j.1460-2075.1995.tb07241.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info A chloroplastic outer envelope membrane protein of 75 kDa (OEP75) was identified previously as a component of the protein import machinery. Here we provide additional evidence that OEP75 is a component of protein import, present the isolation of a cDNA clone encoding this protein, briefly describe its developmental expression and tissue specificity, and characterize its insertion into the outer envelope membrane. OEP75 was synthesized as a higher molecular weight precursor (prOEP75) which bound to isolated chloroplasts in an in vitro import assay and subsequently was processed to the mature form (mOEP75). During this import assay, two proteins intermediate in size between prOEP75 and mOEP75 were detected. One of these intermediates was also detected in chloroplast envelopes isolated from young pea leaves. Binding and processing of prOEP75 required ATP and one or more surface-exposed proteinaceous components, and was competed by prSSU, a stromal-targeted protein. We propose that the N-terminus of the prOEP75 transit peptide acts as a stromal-targeting domain and a central, hydrophobic region of this transit peptide acts as a stop-transfer domain. A complex route of insertion and processing of prOEP75 may exist to ensure high fidelity targeting of this import component. Previous ArticleNext Article Volume 14Issue 111 June 1995In this issue RelatedDetailsLoading ...

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