ArticleJournal of bacteriology2003
A SecE mutation that modulates SecY-SecE translocase assembly, identified as a specific suppressor of SecY defects.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Identification and characterization of a translation arrest motif in VemP by systematic mutational analysis.The Journal of biological chemistry · 2018Article
- Nascent chain-monitored remodeling of the Sec machinery for salinity adaptation of marine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Conformational variation of the translocon enhancing chaperone SecDF.Journal of structural and functional genomics · 2014Article
- Dynamics of SecY translocons with translocation-defective mutations.Structure (London, England : 1993) · 2010Article
- Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Purification, crystallization and preliminary X-ray diffraction of SecDF, a translocon-associated membrane protein, from Thermus thermophilus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2006Article
- Mutational analysis of transmembrane regions 3 and 4 of SecY, a central component of protein translocase.Journal of bacteriology · 2004Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The SecY39(Cs) (cold-sensitive) alteration of Arg357 results in a defect of translocation initiation. As a means to dissect the Sec translocation machinery, we isolated mutations that act as suppressors of the secY39 defect. A specific secE mutation, designated secE105, was thus isolated. This mutation proved to be identical with the prlG2 mutation and to suppress a number of cold-sensitive secY mutations. However, other prlG mutations did not effectively suppress the secY defects. Evidence indicates that the Ser105-to-Pro alteration in the C-terminal transmembrane segment of SecE weakens SecY-SecE association. In vitro analyses showed that the SecE(S105P) alteration preferentially stimulates the initial phase of translocation. It is suggested that the S105P alteration affects the SecYEG channel such that it is more prone to open and to accept the translocation initiation domain of a preprotein molecule.
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