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YdiV: a dual function protein that targets FlhDC for ClpXP-dependent degradation by promoting release of DNA-bound FlhDC complex.
Mol Microbiol. 2012 Mar; 83(6):1268-84.MM

Abstract

YdiV is an EAL-like protein that acts as a post-transcriptional, negative regulator of the flagellar master transcriptional activator complex, FlhD(4)C(2), in Salmonella enterica to couple flagellar gene expression to nutrient availability. Mutants defective in ClpXP protease no longer exhibit YdiV-dependent inhibition of FlhD(4)C(2)-dependent transcription under moderate YdiV expression conditions. ClpXP protease degrades FlhD(4)C(2), and this degradation is accelerated in the presence of YdiV. YdiV complexed with both free and DNA-bound FlhD(4)C(2); and stripped FlhD(4)C(2) from DNA. A L22H substitution in FlhD was isolated as insensitive to YdiV inhibition. The FlhD L22H substitution prevented the interaction of YdiV with free FlhD(4)C(2) and the ability of YdiV to release FlhD(4)C(2) bound to DNA. These results demonstrate that YdiV prevents FlhD(4)C(2)-dependent flagellar gene transcription and acts as a putative adaptor to target FlhD(4)C(2) for ClpXP-dependent proteolysis. Our results suggest that YdiV is an EAL-like protein that has evolved from a dicyclic-GMP phosphodiesterase into a dual-function regulatory protein that connects flagellar gene expression to nutrient starvation.

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Authors+Show Affiliations

Takaya A
Department of Microbiology and Molecular Genetics, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba, 260-8675 Japan.
Erhardt M
No affiliation info available
Karata K
No affiliation info available
Winterberg K
No affiliation info available
Yamamoto T
No affiliation info available
Hughes KT
No affiliation info available

MeSH

Bacterial ProteinsBinding SitesDNA, BacterialEndopeptidase ClpFlagellaGene Expression Regulation, BacterialPromoter Regions, GeneticProtein BindingProteolysisSalmonella typhimuriumTrans-ActivatorsTranscription, Genetic

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

22380597

Citation

Takaya, Akiko, et al. "YdiV: a Dual Function Protein That Targets FlhDC for ClpXP-dependent Degradation By Promoting Release of DNA-bound FlhDC Complex." Molecular Microbiology, vol. 83, no. 6, 2012, pp. 1268-84.
Takaya A, Erhardt M, Karata K, et al. YdiV: a dual function protein that targets FlhDC for ClpXP-dependent degradation by promoting release of DNA-bound FlhDC complex. Mol Microbiol. 2012;83(6):1268-84.
Takaya, A., Erhardt, M., Karata, K., Winterberg, K., Yamamoto, T., & Hughes, K. T. (2012). YdiV: a dual function protein that targets FlhDC for ClpXP-dependent degradation by promoting release of DNA-bound FlhDC complex. Molecular Microbiology, 83(6), 1268-84. https://doi.org/10.1111/j.1365-2958.2012.08007.x
Takaya A, et al. YdiV: a Dual Function Protein That Targets FlhDC for ClpXP-dependent Degradation By Promoting Release of DNA-bound FlhDC Complex. Mol Microbiol. 2012;83(6):1268-84. PubMed PMID: 22380597.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - YdiV: a dual function protein that targets FlhDC for ClpXP-dependent degradation by promoting release of DNA-bound FlhDC complex. AU - Takaya,Akiko, AU - Erhardt,Marc, AU - Karata,Kiyonobu, AU - Winterberg,Kelly, AU - Yamamoto,Tomoko, AU - Hughes,Kelly T, Y1 - 2012/03/02/ PY - 2012/3/3/entrez PY - 2012/3/3/pubmed PY - 2012/8/11/medline SP - 1268 EP - 84 JF - Molecular microbiology JO - Mol Microbiol VL - 83 IS - 6 N2 - YdiV is an EAL-like protein that acts as a post-transcriptional, negative regulator of the flagellar master transcriptional activator complex, FlhD(4)C(2), in Salmonella enterica to couple flagellar gene expression to nutrient availability. Mutants defective in ClpXP protease no longer exhibit YdiV-dependent inhibition of FlhD(4)C(2)-dependent transcription under moderate YdiV expression conditions. ClpXP protease degrades FlhD(4)C(2), and this degradation is accelerated in the presence of YdiV. YdiV complexed with both free and DNA-bound FlhD(4)C(2); and stripped FlhD(4)C(2) from DNA. A L22H substitution in FlhD was isolated as insensitive to YdiV inhibition. The FlhD L22H substitution prevented the interaction of YdiV with free FlhD(4)C(2) and the ability of YdiV to release FlhD(4)C(2) bound to DNA. These results demonstrate that YdiV prevents FlhD(4)C(2)-dependent flagellar gene transcription and acts as a putative adaptor to target FlhD(4)C(2) for ClpXP-dependent proteolysis. Our results suggest that YdiV is an EAL-like protein that has evolved from a dicyclic-GMP phosphodiesterase into a dual-function regulatory protein that connects flagellar gene expression to nutrient starvation. SN - 1365-2958 UR - https://www.unboundmedicine.com/medline/citation/22380597/YdiV:_a_dual_function_protein_that_targets_FlhDC_for_ClpXP_dependent_degradation_by_promoting_release_of_DNA_bound_FlhDC_complex_ L2 - https://doi.org/10.1111/j.1365-2958.2012.08007.x DB - PRIME DP - Unbound Medicine ER -