Translation arrest of SecM is essential for the basal and regulated expression of SecA. - Wikidata - awgldk - TriplyDB

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

http://www.wikidata.org/entity/Q37483786

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Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection SecM facilitates translocase function of SecA by localizing its biosynthesis Nascentome analysis uncovers futile protein synthesis in Escherichia coli Recruitment of a species-specific translational arrest module to monitor different cellular processes.The translational regulatory function of SecM requires the precise timing of membrane targeting.Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.Divergent protein motifs direct elongation factor P-mediated translational regulation in Salmonella enterica and Escherichia coli.Mutations in the Escherichia coli ribosomal protein L22 selectively suppress the expression of a secreted bacterial virulence factor.Divergent stalling sequences sense and control cellular physiology.The ribosome and its role in protein folding: looking through a magnifying glass.SsrA tagging of Escherichia coli SecM at its translation arrest sequence.Prolyl-tRNA(Pro) in the A-site of SecM-arrested ribosomes inhibits the recruitment of transfer-messenger RNA.Functional defects in transfer RNAs lead to the accumulation of ribosomal RNA precursors.MifM monitors total YidC activities of Bacillus subtilis, including that of YidC2, the target of regulation.Identification and characterization of a translation arrest motif in VemP by systematic mutational analysis.Genome scale analysis ofEscherichia coliwith a comprehensive prokaryotic sequence-based biophysical model of translation initiation and elongation.The Essential Genome of Escherichia coli K-12.The long alpha-helix of SecA is important for the ATPase coupling of translocation.Disruption of rpmJ encoding ribosomal protein L36 decreases the expression of secY upstream of the spc operon and inhibits protein translocation in Escherichia coli.Identification of a hyperactive variant of the SecM motif involved in ribosomal arrest.Cell biology. A translational pause to localize.Ribosome-based protein folding systems are structurally divergent but functionally universal across biological kingdoms.

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Translation arrest of SecM is essential for the basal and regulated expression of SecA.

http://www.wikidata.org/entity/Q37483786

description

article científic

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article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 09 August 2004

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

@en

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

@nl

type

label

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

@en

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

@nl

prefLabel

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

@en

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

@nl

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PNAS.0404907101

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Translation arrest of SecM is essential for the basal and regulated expression of SecA.

@en

P2093

Akiko Murakami

http://www.w3.org/2001/XMLSchema#string

Koreaki Ito

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P2860

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

X-ray structure of a protein-conducting channel

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli.

Secretion monitor, SecM, undergoes self-translation arrest in the cytosol.

Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon.

Oxazolidinone resistance mutations in 23S rRNA of Escherichia coli reveal the central region of domain V as the primary site of drug action.

Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery.

The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself.

The ribosomal exit tunnel functions as a discriminating gate.

P304

12330-12335

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scholarly article

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10.1073/PNAS.0404907101

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33

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101

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Hitoshi Nakatogawa

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2004-08-09T00:00:00Z

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8408095

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514405

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