The nascent polypeptide‐associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo

FEBS Letters

George, Rebecca²  Beddoe, Travis¹  Lithgow, Trevor¹  Walsh, Peter¹ 

[1] Russell Grimwade School of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Vic. 3010, Australia;Department of Biochemistry, La Trobe University, Bundoora 3083, Australia

关键词: Ribosome;    Mitochondrion;    Protein targeting;    Nascent chain;    SRP;    signal recognition particle;    TOM complex;    translocase in the outer mitochondrial membrane;    NAC;    nascent polypeptide-associated complex;    SDS-PAGE;    sodium dodecyl sulfate polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(02)02528-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The nascent polypeptide-associated complex (NAC) is a peripheral component of cytoplasmic ribosomes, and interacts with nascent chains as they leave the ribosome. Yeast mutants lacking NAC translate polypeptides normally, but have fewer ribosomes associated with the mitochondrial surface. The mutants lacking NAC suffer mitochondrial defects and have decreased levels of proteins like fumarase, normally targeted to mitochondria co-translationally. NAC might contribute to a ribosomal environment in which amino-terminal, mitochondrial targeting sequences can effectively adopt their appropriate conformation.

【 授权许可】

Unknown