Puf6 and Loc1 Are the Dedicated Chaperones of Ribosomal Protein Rpl43 in Saccharomyces cerevisiae

Autor: Kai-Yin Lo, Jui-Sheng Lai, Ning-Hsiang Hsu, Kai-Jen Liang, Le-Yun Yueh
Jazyk: angličtina
Rok vydání: 2019
Předmět:
0301 basic medicine
Models
Molecular

Ribosomal Proteins
Saccharomyces cerevisiae Proteins
Protein Conformation
Protein subunit
Ribosome biogenesis
ribosome biogenesis
Saccharomyces cerevisiae
Karyopherins
Ribosome
Catalysis
Article
Inorganic Chemistry
03 medical and health sciences
0302 clinical medicine
Ribosomal protein
Gene Expression Regulation
Fungal

chaperone
Physical and Theoretical Chemistry
Molecular Biology
Spectroscopy
Binding Sites
biology
Chemistry
Eukaryotic Large Ribosomal Subunit
Protein Stability
Organic Chemistry
RNA
Nuclear Proteins
RNA-Binding Proteins
General Medicine
Computer Science Applications
Cell biology
030104 developmental biology
Chaperone (protein)
Multiprotein Complexes
Mutation
biology.protein
transacting factors
030217 neurology & neurosurgery
Protein Binding
Zdroj: International Journal of Molecular Sciences
Volume 20
Issue 23
ISSN: 1422-0067
Popis: Ribosomal proteins are highly expressed, and the quality of ribosomal proteins must be rigorously controlled to build up a functional ribosome. Rpl43, ribosomal protein large subunit 43, is located nearby the E-site of ribosomes. In our previous study, we found that Puf6, Loc1, and Rpl43 form a trimeric complex in Saccharomyces cerevisiae. Rpl43 protein levels are under-accumulated in the absence of PUF6 or LOC1. However, why the loss of Puf6 or Loc1 decreased the protein levels of Rpl43 remained unclear. In the present study, we further dissected the connections among these three proteins and found that the processing defects of pre-ribosomal RNA in puf6&Delta
and loc1&Delta
are similar to those of the mutant with depletion of Rpl43. The stability of newly synthesized Rpl43 protein decreased slightly in puf6&Delta
and significantly in loc1&Delta
We also found that Puf6 and Loc1 could interact with nascent Rpl43 co-translationally via the N-terminus of Rpl43. While the association and dissociation of Rpl43 with karyopherins did not depend on Puf6 and Loc1, Puf6 and Loc1 interacted with nascent Rpl43 in collaboration. While the N-terminus of Puf6 contained nuclear localization signals for transport, the PUF (Pumilio) domain was essential to interaction with Loc1, Rpl43, and 60S subunits. The C-terminus of Loc1 is more important for interaction with Puf6 and Rpl43. In this study, we found that Puf6 and Loc1 are the dedicated chaperones of ribosomal protein Rpl43 and also analyzed the potential interaction domains among the three proteins. Correct formation of the Puf6, Loc1, and Rpl43 ternary complex is required to properly proceed to the next step in 60S biogenesis.
Databáze: OpenAIRE
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