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Effect of amino acid substitutions in the GerAA protein on the function of the alanine-responsive germinant receptor of Bacillus subtilis spores

Effect of amino acid substitutions in the GerAA protein on the function of the alanine-responsive germinant receptor of Bacillus subtilis spores
Effect of amino acid substitutions in the GerAA protein on the function of the alanine-responsive germinant receptor of Bacillus subtilis spores

Spores of Bacillus subtilis require the GerAA, GerAB, and GerAC receptor proteins for L-alanine-induced germination. Mutations in gerAA, both random and site directed, result in phenotypes that identify amino acid residues important for receptor function in broad terms. They highlight the functional importance of two regions in the central, integral membrane domain of GerAA. A P324S substitution in the first residue of a conserved PFPP motif results in a 10-fold increase in a spore's sensitivity to alanine; a P326S change results in the release of phase-dark spores, in which the receptor may be in an "activated" or "quasigerminated" state. Substitutions in residues 398 to 400, in a short loop between the last two likely membrane-spanning helices of this central domain, all affect the germination response, with the G398S substitution causing a temperature-sensitive defect. In others, there are wider effects on the receptor: if alanine is substituted for conserved residue N146, H304, or E330, a severe defect in L-alanine germination results. This correlates with the absence of GerAC, suggesting that the assembly or stability of the entire receptor complex has been compromised by the defect in GerAA. In contrast, severely germination-defective mutants such as E129K, L373F, S400F, and M409N mutants retain GerAC at normal levels, suggesting more local and specific effects on the function of GerAA itself. Further interpretation will depend on progress in structural analysis of the receptor proteins.

Alanine, Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Bacillus subtilis, Bacterial Proteins, Conserved Sequence, Gene Expression Regulation, Bacterial, Membrane Proteins, Molecular Sequence Annotation, Phenotype, Point Mutation, Spores, Bacterial, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
0021-9193
2268-75
Mongkolthanaruk, Wiyada
dd6afeb4-6232-4b72-9eeb-8bad116c5eca
Cooper, Gareth R.
5ad017f5-a7f9-43b9-9f78-a4962d5629a9
Mawer, Julia S.P.
3cb98917-00d5-428e-8bf2-5d4e73cbee1f
Allan, Raymond N.
390a7d0a-38e1-410a-8dfe-c8ef8408f5e1
Moir, Anne
202c7ab8-0d49-46fe-a872-d09dfff30169
Mongkolthanaruk, Wiyada
dd6afeb4-6232-4b72-9eeb-8bad116c5eca
Cooper, Gareth R.
5ad017f5-a7f9-43b9-9f78-a4962d5629a9
Mawer, Julia S.P.
3cb98917-00d5-428e-8bf2-5d4e73cbee1f
Allan, Raymond N.
390a7d0a-38e1-410a-8dfe-c8ef8408f5e1
Moir, Anne
202c7ab8-0d49-46fe-a872-d09dfff30169

Mongkolthanaruk, Wiyada, Cooper, Gareth R., Mawer, Julia S.P., Allan, Raymond N. and Moir, Anne (2011) Effect of amino acid substitutions in the GerAA protein on the function of the alanine-responsive germinant receptor of Bacillus subtilis spores. Journal of Bacteriology, 193 (9), 2268-75. (doi:10.1128/JB.01398-10).

Record type: Article

Abstract

Spores of Bacillus subtilis require the GerAA, GerAB, and GerAC receptor proteins for L-alanine-induced germination. Mutations in gerAA, both random and site directed, result in phenotypes that identify amino acid residues important for receptor function in broad terms. They highlight the functional importance of two regions in the central, integral membrane domain of GerAA. A P324S substitution in the first residue of a conserved PFPP motif results in a 10-fold increase in a spore's sensitivity to alanine; a P326S change results in the release of phase-dark spores, in which the receptor may be in an "activated" or "quasigerminated" state. Substitutions in residues 398 to 400, in a short loop between the last two likely membrane-spanning helices of this central domain, all affect the germination response, with the G398S substitution causing a temperature-sensitive defect. In others, there are wider effects on the receptor: if alanine is substituted for conserved residue N146, H304, or E330, a severe defect in L-alanine germination results. This correlates with the absence of GerAC, suggesting that the assembly or stability of the entire receptor complex has been compromised by the defect in GerAA. In contrast, severely germination-defective mutants such as E129K, L373F, S400F, and M409N mutants retain GerAC at normal levels, suggesting more local and specific effects on the function of GerAA itself. Further interpretation will depend on progress in structural analysis of the receptor proteins.

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More information

e-pub ahead of print date: 4 March 2011
Published date: May 2011
Keywords: Alanine, Amino Acid Motifs, Amino Acid Sequence, Amino Acid Substitution, Bacillus subtilis, Bacterial Proteins, Conserved Sequence, Gene Expression Regulation, Bacterial, Membrane Proteins, Molecular Sequence Annotation, Phenotype, Point Mutation, Spores, Bacterial, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
Organisations: Biomedicine

Identifiers

Local EPrints ID: 406446
URI: https://eprints.soton.ac.uk/id/eprint/406446
ISSN: 0021-9193
PURE UUID: 28322a3b-f832-4683-9f4b-be80da5c50f1

Catalogue record

Date deposited: 10 Mar 2017 10:47
Last modified: 15 Jul 2019 18:32

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