The Yeast Ccr4-Not Complex Controls Ubiquitination of the Nascent-associated Polypeptide (NAC-EGD) Complex
نویسندگان
چکیده
منابع مشابه
Nascent polypeptide-associated complex stimulates protein import into yeast mitochondria.
To identify yeast cytosolic proteins that mediate targeting of precursor proteins to mitochondria, we developed an in vitro import system consisting of purified yeast mitochondria and a radiolabeled mitochondrial precursor protein whose C terminus was still attached to the ribosome. In this system, the N terminus of the nascent chain was translocated across both mitochondrial membranes, generat...
متن کاملA dual function for chaperones SSB–RAC and the NAC nascent polypeptide–associated complex on ribosomes
The yeast Hsp70/40 system SSB-RAC (stress 70 B-ribosome-associated complex) binds to ribosomes and contacts nascent polypeptides to assist cotranslational folding. In this study, we demonstrate that nascent polypeptide-associated complex (NAC), another ribosome-tethered system, is functionally connected to SSB-RAC and the cytosolic Hsp70 network. Simultaneous deletions of genes encoding NAC and...
متن کاملRibosome association and stability of the nascent polypeptide-associated complex is dependent upon its own ubiquitination.
In this work we addressed the role of ubiquitination in the function of the nascent polypeptide-associated complex (NAC), named EGD in the yeast Saccharomyces cerevisiae. To this end, we first identified the lysines residues required for ubiquitination of EGD/NAC. While simultaneous mutation of many lysines in the alpha-subunit of NAC (Egd2p) was required to abolish its ubiquitination, for the ...
متن کاملThe yeast nascent polypeptide-associated complex initiates protein targeting to mitochondria in vivo.
The yeast nascent polypeptide-associated complex (NAC) is encoded by two genes, EGD1 and EGD2, and is associated with cytoplasmic ribosomes. Yeast mutants lacking NAC (Deltaegd2) are viable but suffer slight defects in the targeting of nascent polypeptides to several locations including the endoplasmic reticulum and mitochondria. If both NAC and Mft52p are missing from yeast cells, inefficient ...
متن کاملDual binding mode of the Nascent Polypeptide-associated Complex (NAC) reveals a novel universal adapter site on the ribosome
Nascent Polypeptide-associated Complex (NAC) was identified in eukaryotes as the first cytosolic factor which contacts the nascent polypeptide chain emerging from the ribosome. NAC is present as a homodimer in Archaea and as a highly conserved heterodimer in eukaryotes. Mutations in NAC cause severe embryonically lethal phenotypes in mice, D. melanogaster and C. elegans. In the yeast Saccharomy...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2006
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)84051-6