Identification and characterization of a translation arrest motif in VemP by systematic mutational analysis-Reference-Cited by-同舟云学术

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Identification and characterization of a translation arrest motif in VemP by systematic mutational analysis

Published:2018-02 Issue:8 Volume:293 Page:2915-2926
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Mori Hiroyuki,Sakashita Sohei,Ito Jun,Ishii Eiji,Akiyama Yoshinori

Funder

Japan Society for the Promotion of Science

Ministry of Education, Culture, Sports, Science and Technology

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference35 articles.

1. The Sec protein-translocation pathway;Mori;Trends Microbiol,2001

2. Structural and mechanistic insights into protein translocation;Rapoport;Annu. Rev. Cell Dev. Biol,2017

3. Genetic and molecular characterization of the Escherichia coli secD operon and its products;Pogliano;J. Bacteriol,1994

4. Tunnel formation inferred from the I-form structures of the proton-driven protein secretion motor SecDF;Furukawa;Cell Rep,2017

5. Structure and function of a membrane component SecDF that enhances protein export;Tsukazaki;Nature,2011

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1. Translation arrest cancellation of VemP, a secretion monitor in Vibrio, is regulated by multiple cis- and trans-factors, including SecY;Journal of Biological Chemistry;2024-09

2. Using yeasts for the studies of nonfunctional factors in protein evolution;Yeast;2024-06-19

3. Nonspecific N-terminal tetrapeptide insertions disrupt the translation arrest induced by ribosome-arresting peptide sequences;Journal of Biological Chemistry;2024-06

4. Effect of translation enhancing nascent SKIK peptide on the arrest peptides containing consecutive Proline;2024-02-29

5. Nascent MSKIK peptide cancels ribosomal stalling by arrest peptides in Escherichia coli;Journal of Biological Chemistry;2023-05

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