A Family of Small Intrinsically Disordered Proteins Involved in Flagellum-Dependent Motility in Salmonella enterica

Author:

Oguri Tamiko1,Kwon Youjeong1,Woo Jerry K. K.1,Prehna Gerd2,Lee Hyun3,Ning Miaoran4,Won Kyoung-Jae4,Lee Jiyoung1,Mei Sally1,Shi Yixin5,Jeong Hyunyoung4,Lee Hyunwoo16

Affiliation:

1. Center for Biomolecular Sciences, University of Illinois at Chicago, Chicago, Illinois, USA

2. Department of Microbiology, University of Manitoba, Winnipeg, Manitoba, Canada

3. Center for Structural Biology, University of Illinois at Chicago, Chicago, Illinois, USA

4. Department of Pharmacy Practice, College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois, USA

5. The School of Life Sciences, Arizona State University, Tempe, Arizona, USA

6. Department of Biopharmaceutical Sciences, College of Pharmacy, University of Illinois at Chicago, Chicago, Illinois, USA

Abstract

This study reports the identification of a novel family of small intrinsically disordered proteins that are conserved in a wide range of flagellated and nonflagellated bacteria. Although this study identifies the role of these small proteins in the scope of flagellum-dependent motility in Salmonella , they likely play larger roles in a more conserved cellular pathway(s) that indirectly affects flagellum expression in the case of motile bacteria. Small intrinsically disordered proteins have not been well characterized in prokaryotes, and the results of our study provide a basis for their detailed functional characterization.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference89 articles.

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3. Macnab R. 1996. Flagella and motility, p 123–145. In Neidhardt FC (ed), Escherichia coli and Salmonella typhimurium: cellular and molecular biology. American Society for Microbiology, Washington, DC.

4. C-ring requirement in flagellar type III secretion is bypassed by FlhDC upregulation

5. Phase variation: Genetic analysis of switching mutants

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