Wyszukiwarka
Functional similarities and differences among subunits of the nascent polypeptide-associated complex (NAC) of Saccharomyces cerevisiae
Abstrakt
Protein factors bind ribosomes near the tunnel exit, facilitating protein trafficking and folding. In eukaryotes, the heterodimeric nascent polypeptide-associated complex (NAC) is the most abundant - equimolar to ribosomes. Saccharomyces cerevisiae has a minor β-type subunit (Nacβ2) in addition to abundant Nacβ1, and therefore two NAC heterodimers, α/β1 and α/β12. The additional beta NAC gene arose at the time of the whole genome duplication that occurred in the S. cerevisiae lineage. Nacβ2 has been implicated in regulating the fate of mRNA encoding ribosomal protein Rpl4 during translation via its interaction with the Caf130 subunit of the regulatory CCR4-Not complex. We found that Nacβ2 residues just C-terminal to the globular domain are required for its interaction with Caf130 and its negative effect on growth of cells lacking Acl4, the specialized chaperone for Rpl4. Substitution of these Nacβ2 residues at homologous positions in Nacβ1 results in a chimeric protein that interacts with Caf130 and slows the growth of ∆acl4 cells lacking Nacβ2. Furthermore, alteration of residues in the N-terminus of Nacβ2 or chimeric Nacβ1 previously shown to affect ribosome binding overcomes the growth defect of ∆acl4. Our results are consistent with a model in which Nacβ2’s ribosome association per se, or its precise positioning, is necessary for productive recruitment of CCR4-Not via its interaction with the Caf130 subunit to drive Rpl4 mRNA degradation.
Cytowania
-
0
CrossRef
-
0
Web of Science
-
0
Scopus
Autorzy (6)
-
Brenda A. Schilke
-
Thomas Ziegelhoffer
-
Jaroslaw Marszalek
-
Bartlomiej Tomiczek
-
Elizabeth Craig
Cytuj jako
Pełna treść
- Wersja publikacji
- Accepted albo Published Version
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1016/j.cstres.2024.10.004
- Licencja
-
otwiera się w nowej karcie
Słowa kluczowe
Informacje szczegółowe
- Kategoria:
- Publikacja w czasopiśmie
- Typ:
- artykuły w czasopismach
- Opublikowano w:
-
CELL STRESS & CHAPERONES
ISSN: 1355-8145 - Język:
- angielski
- Rok wydania:
- 2024
- Opis bibliograficzny:
- Schilke B. A., Ziegelhoffer T., Domański P., Marszalek J., Tomiczek B., Craig E.: Functional similarities and differences among subunits of the nascent polypeptide-associated complex (NAC) of Saccharomyces cerevisiae// CELL STRESS & CHAPERONES -, (2024),
- DOI:
- Cyfrowy identyfikator dokumentu elektronicznego (otwiera się w nowej karcie) 10.1016/j.cstres.2024.10.004
- Źródła finansowania:
-
- This study was supported by grants from the National Institutes of Health [R35 GM127009 to E.A.C.] and National Science Center, Poland [OPUS 21 2021/41/B/NZ8/02835 to B.T.].
- Weryfikacja:
- Politechnika Gdańska
wyświetlono 4 razy
Publikacje, które mogą cię zainteresować
Iron–Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of Mutational Robustness of a Highly Specific Protein–Protein Interaction
- W. Delewski,
- B. Paterkiewicz,
- M. Manicki
- + 8 autorów
Analysis of Reconstituted Tripartite Complex Supports Avidity-based Recruitment of Hsp70 by Substrate Bound J-domain Protein
- M. Jelen,
- I. Grochowina,
- A. Grabinska-Rogala
- + 11 autorów
Structure and evolution of the 4-helix bundle domain of Zuotin, a J-domain protein co-chaperone of Hsp70
- O. Shrestha,
- R. Sharma,
- B. Tomiczek
- + 10 autorów