Publication

Bacillus subtilis SpoIIIJ and YqjG function in membrane protein biogenesis.

Saller, M. J., Fusetti, F. & Driessen, A. J. M., Nov-2009, In : Journal of Bacteriology. 191, 21, p. 6749-6757 9 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Saller, M. J., Fusetti, F., & Driessen, A. J. M. (2009). Bacillus subtilis SpoIIIJ and YqjG function in membrane protein biogenesis. Journal of Bacteriology, 191(21), 6749-6757. https://doi.org/10.1128/JB.00853-09

Author

Saller, Manfred J. ; Fusetti, Fabrizia ; Driessen, Arnold J. M. / Bacillus subtilis SpoIIIJ and YqjG function in membrane protein biogenesis. In: Journal of Bacteriology. 2009 ; Vol. 191, No. 21. pp. 6749-6757.

Harvard

Saller, MJ, Fusetti, F & Driessen, AJM 2009, 'Bacillus subtilis SpoIIIJ and YqjG function in membrane protein biogenesis.', Journal of Bacteriology, vol. 191, no. 21, pp. 6749-6757. https://doi.org/10.1128/JB.00853-09

Standard

Bacillus subtilis SpoIIIJ and YqjG function in membrane protein biogenesis. / Saller, Manfred J.; Fusetti, Fabrizia; Driessen, Arnold J. M.

In: Journal of Bacteriology, Vol. 191, No. 21, 11.2009, p. 6749-6757.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Saller MJ, Fusetti F, Driessen AJM. Bacillus subtilis SpoIIIJ and YqjG function in membrane protein biogenesis. Journal of Bacteriology. 2009 Nov;191(21):6749-6757. https://doi.org/10.1128/JB.00853-09


BibTeX

@article{ce732c8d3e174a70bd47d3ce0a4b3492,
title = "Bacillus subtilis SpoIIIJ and YqjG function in membrane protein biogenesis.",
abstract = "In all domains of life Oxa1p-like proteins are involved in membrane protein biogenesis. Bacillus subtilis, a model organism for gram-positive bacteria, contains two Oxa1p homologs: SpoIIIJ and YqjG. These molecules appear to be mutually exchangeable, although SpoIIIJ is specifically required for spore formation. SpoIIIJ and YqjG have been implicated in a posttranslocational stage of protein secretion. Here we show that the expression of either spoIIIJ or yqjG functionally compensates for the defects in membrane insertion due to YidC depletion in Escherichia coli. Both SpoIIIJ and YqjG complement the function of YidC in SecYEG-dependent and -independent membrane insertion of subunits of the cytochrome o oxidase and F(1)F(o) ATP synthase complexes. Furthermore, SpoIIIJ and YqjG facilitate membrane insertion of F(1)F(o) ATP synthase subunit c from both E. coli and B. subtilis into inner membrane vesicles of E. coli. When isolated from B. subtilis cells, SpoIIIJ and YqjG were found to be associated with the entire F(1)F(o) ATP synthase complex, suggesting that they have a role late in the membrane assembly process. These data demonstrate that the Bacillus Oxa1p homologs have a role in membrane protein biogenesis rather than in protein secretion.",
keywords = "ESCHERICHIA-COLI YIDC, F1F0 ATP SYNTHASE, INNER MEMBRANE, SUBUNIT-C, EXPRESSION SYSTEM, BACTERIAL YIDC, INSERTION, COMPLEXES, GENE, TRANSLOCASE",
author = "Saller, {Manfred J.} and Fabrizia Fusetti and Driessen, {Arnold J. M.}",
year = "2009",
month = nov,
doi = "10.1128/JB.00853-09",
language = "English",
volume = "191",
pages = "6749--6757",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "AMER SOC MICROBIOLOGY",
number = "21",

}

RIS

TY - JOUR

T1 - Bacillus subtilis SpoIIIJ and YqjG function in membrane protein biogenesis.

AU - Saller, Manfred J.

AU - Fusetti, Fabrizia

AU - Driessen, Arnold J. M.

PY - 2009/11

Y1 - 2009/11

N2 - In all domains of life Oxa1p-like proteins are involved in membrane protein biogenesis. Bacillus subtilis, a model organism for gram-positive bacteria, contains two Oxa1p homologs: SpoIIIJ and YqjG. These molecules appear to be mutually exchangeable, although SpoIIIJ is specifically required for spore formation. SpoIIIJ and YqjG have been implicated in a posttranslocational stage of protein secretion. Here we show that the expression of either spoIIIJ or yqjG functionally compensates for the defects in membrane insertion due to YidC depletion in Escherichia coli. Both SpoIIIJ and YqjG complement the function of YidC in SecYEG-dependent and -independent membrane insertion of subunits of the cytochrome o oxidase and F(1)F(o) ATP synthase complexes. Furthermore, SpoIIIJ and YqjG facilitate membrane insertion of F(1)F(o) ATP synthase subunit c from both E. coli and B. subtilis into inner membrane vesicles of E. coli. When isolated from B. subtilis cells, SpoIIIJ and YqjG were found to be associated with the entire F(1)F(o) ATP synthase complex, suggesting that they have a role late in the membrane assembly process. These data demonstrate that the Bacillus Oxa1p homologs have a role in membrane protein biogenesis rather than in protein secretion.

AB - In all domains of life Oxa1p-like proteins are involved in membrane protein biogenesis. Bacillus subtilis, a model organism for gram-positive bacteria, contains two Oxa1p homologs: SpoIIIJ and YqjG. These molecules appear to be mutually exchangeable, although SpoIIIJ is specifically required for spore formation. SpoIIIJ and YqjG have been implicated in a posttranslocational stage of protein secretion. Here we show that the expression of either spoIIIJ or yqjG functionally compensates for the defects in membrane insertion due to YidC depletion in Escherichia coli. Both SpoIIIJ and YqjG complement the function of YidC in SecYEG-dependent and -independent membrane insertion of subunits of the cytochrome o oxidase and F(1)F(o) ATP synthase complexes. Furthermore, SpoIIIJ and YqjG facilitate membrane insertion of F(1)F(o) ATP synthase subunit c from both E. coli and B. subtilis into inner membrane vesicles of E. coli. When isolated from B. subtilis cells, SpoIIIJ and YqjG were found to be associated with the entire F(1)F(o) ATP synthase complex, suggesting that they have a role late in the membrane assembly process. These data demonstrate that the Bacillus Oxa1p homologs have a role in membrane protein biogenesis rather than in protein secretion.

KW - ESCHERICHIA-COLI YIDC

KW - F1F0 ATP SYNTHASE

KW - INNER MEMBRANE

KW - SUBUNIT-C

KW - EXPRESSION SYSTEM

KW - BACTERIAL YIDC

KW - INSERTION

KW - COMPLEXES

KW - GENE

KW - TRANSLOCASE

U2 - 10.1128/JB.00853-09

DO - 10.1128/JB.00853-09

M3 - Article

VL - 191

SP - 6749

EP - 6757

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 21

ER -

ID: 1927488