Folding of CFTR Is Predominantly Cotranslational
2005; Elsevier BV; Volume: 20; Issue: 2 Linguagem: Inglês
10.1016/j.molcel.2005.09.007
ISSN1097-4164
AutoresBertrand Kleizen, Thijs van Vlijmen, Hugo R. de Jonge, Ineke Braakman,
Tópico(s)Bacterial Genetics and Biotechnology
ResumoThe folding process for newly synthesized, multispanning membrane proteins in the endoplasmic reticulum (ER) is largely unknown. Here, we describe early folding events of the cystic fibrosis transmembrane conductance regulator (CFTR), a member of the ABC-transporter family. In vitro translation of CFTR in the presence of semipermeabilized cells allowed us to investigate this protein during nascent chain elongation. We found that CFTR folds mostly during synthesis as determined by protease susceptibility. C-terminally truncated constructs showed that individual CFTR domains formed well-defined structures independent of C-terminal parts. We conclude that the multidomain protein CFTR folds mostly cotranslationally, domain by domain.
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