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PMID: 10836794 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Mtt1 is a Upf1-like helicase that interacts with the translation termination factors and whose overexpression can modulate termination efficiency.

RNA (New York, N.Y.) ·Vol. 6 ·No. 5 ·2000-05-00 ·Pages 730-43

Czaplinski K, Majlesi N, Banerjee T, Peltz SW

Abstract

Translation termination is the final step that completes the synthesis of a polypeptide. Premature translation termination by introduction of a nonsense mutation leads to the synthesis of a truncated protein. We report the identification and characterization of the product of the MTT1 gene, a helicase belonging to the Upfl-like family of helicases that is involved in modulating translation termination. MTT1 is homologous to UPF1, a factor previously shown to function in both mRNA turnover and translation termination. Overexpression of MTT1 induced a nonsense suppression phenotype in a wild-type yeast strain. Nonsense suppression is apparently not due to induction of [PSI+], even though cooverexpression of HSP104 alleviated the nonsense suppression phenotype observed in cells overexpressing MTT1, suggesting a more direct role of Hsp104p in the translation termination process. The MTT1 gene product was shown to interact with translation termination factors and is localized to polysomes. Taken together, these results indicate that at least two members of a family of RNA helicases modulate translation termination efficiency in cells.

MeSH Terms
Adenosine Triphosphatases Amino Acid Sequence Animals DNA Helicases Evolution, Molecular Gene Expression Genes, Fungal Humans Molecular Sequence Data Peptide Chain Termination, Translational Peptide Termination Factors/metabolism Polyribosomes/metabolism RNA Helicases/classification,genetics,metabolism RNA, Fungal/genetics,metabolism RNA, Messenger/genetics,metabolism Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Suppression, Genetic Trans-Activators
Chemicals
Peptide Termination Factors RNA, Fungal RNA, Messenger Saccharomyces cerevisiae Proteins Trans-Activators peptide-chain-release factor 3 Adenosine Triphosphatases NAM7 protein, S cerevisiae DNA Helicases RNA Helicases UPF1 protein, human ECM32 protein, S cerevisiae
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Czaplinski K
Department of Molecular Genetics and Microbiology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854, USA.
Majlesi N
Banerjee T
Peltz S W
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Article Info
Journal
RNA (New York, N.Y.)
Abbr.
RNA
ISSN
1355-8382
DOI
10.1017/s1355838200992392
Published
2000-05-00
Pages
730-43
Language
English
Region
United States
NLM ID
9509184
PMCID
PMC1369953
Subset
IM
Grants
NIGMS NIH HHS · GM48631 · United States
External Links
PubMed source DOI: 10.1017/s1355838200992392 PMC Full Text View journal details
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