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SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins.
J Biol Chem 1998; 273(33):21217-24JB

Abstract

In the present studies, we show that the SecD and SecF equivalents of the Gram-positive bacterium Bacillus subtilis are jointly present in one polypeptide, denoted SecDF, that is required to maintain a high capacity for protein secretion. Unlike the SecD subunit of the pre-protein translocase of Escherichia coli, SecDF of B. subtilis was not required for the release of a mature secretory protein from the membrane, indicating that SecDF is involved in earlier translocation steps. Strains lacking intact SecDF showed a cold-sensitive phenotype, which was exacerbated by high level production of secretory proteins, indicating that protein translocation in B. subtilis is intrinsically cold-sensitive. Comparison with SecD and SecF proteins from other organisms revealed the presence of 10 conserved regions in SecDF, some of which appear to be important for SecDF function. Interestingly, the SecDF protein of B. subtilis has 12 putative transmembrane domains. Thus, SecDF does not only show sequence similarity but also structural similarity to secondary solute transporters. Our data suggest that SecDF of B. subtilis represents a novel type of the SecD and SecF proteins, which seems to be present in at least two other organisms.

Authors+Show Affiliations

Department of Genetics, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Kerklaan 30, 9751 NN Haren, The Netherlands.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

9694879

Citation

Bolhuis, A, et al. "SecDF of Bacillus Subtilis, a Molecular Siamese Twin Required for the Efficient Secretion of Proteins." The Journal of Biological Chemistry, vol. 273, no. 33, 1998, pp. 21217-24.
Bolhuis A, Broekhuizen CP, Sorokin A, et al. SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins. J Biol Chem. 1998;273(33):21217-24.
Bolhuis, A., Broekhuizen, C. P., Sorokin, A., van Roosmalen, M. L., Venema, G., Bron, S., ... van Dijl, J. M. (1998). SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins. The Journal of Biological Chemistry, 273(33), pp. 21217-24.
Bolhuis A, et al. SecDF of Bacillus Subtilis, a Molecular Siamese Twin Required for the Efficient Secretion of Proteins. J Biol Chem. 1998 Aug 14;273(33):21217-24. PubMed PMID: 9694879.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins. AU - Bolhuis,A, AU - Broekhuizen,C P, AU - Sorokin,A, AU - van Roosmalen,M L, AU - Venema,G, AU - Bron,S, AU - Quax,W J, AU - van Dijl,J M, PY - 1998/8/8/pubmed PY - 1998/8/8/medline PY - 1998/8/8/entrez SP - 21217 EP - 24 JF - The Journal of biological chemistry JO - J. Biol. Chem. VL - 273 IS - 33 N2 - In the present studies, we show that the SecD and SecF equivalents of the Gram-positive bacterium Bacillus subtilis are jointly present in one polypeptide, denoted SecDF, that is required to maintain a high capacity for protein secretion. Unlike the SecD subunit of the pre-protein translocase of Escherichia coli, SecDF of B. subtilis was not required for the release of a mature secretory protein from the membrane, indicating that SecDF is involved in earlier translocation steps. Strains lacking intact SecDF showed a cold-sensitive phenotype, which was exacerbated by high level production of secretory proteins, indicating that protein translocation in B. subtilis is intrinsically cold-sensitive. Comparison with SecD and SecF proteins from other organisms revealed the presence of 10 conserved regions in SecDF, some of which appear to be important for SecDF function. Interestingly, the SecDF protein of B. subtilis has 12 putative transmembrane domains. Thus, SecDF does not only show sequence similarity but also structural similarity to secondary solute transporters. Our data suggest that SecDF of B. subtilis represents a novel type of the SecD and SecF proteins, which seems to be present in at least two other organisms. SN - 0021-9258 UR - https://www.unboundmedicine.com/medline/citation/9694879/SecDF_of_Bacillus_subtilis_a_molecular_Siamese_twin_required_for_the_efficient_secretion_of_proteins_ L2 - http://www.jbc.org/cgi/pmidlookup?view=long&pmid=9694879 DB - PRIME DP - Unbound Medicine ER -