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The nascent polypeptide‐associated complex (NAC) promotes interaction of ribosomes with the mitochondrial surface in vivo
Author(s) -
George Rebecca,
Walsh Peter,
Beddoe Travis,
Lithgow Trevor
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02528-0
Subject(s) - ribosome , mitochondrion , mitochondrial ribosome , mutant , cytoplasm , microbiology and biotechnology , ribosomal protein , eukaryotic ribosome , ribosomal rna , biochemistry , biology , chemistry , rna , gene
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.