Dps Is a Universally Conserved Dual-Action DNA-Binding and Ferritin Protein-Reference-Cited by-同舟云学术

Dps Is a Universally Conserved Dual-Action DNA-Binding and Ferritin Protein

Published:2022-05-17 Issue:5 Volume:204 Page:
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Orban Katie¹,Finkel Steven E.¹^ORCID

Affiliation:

1. Molecular and Computational Biology Section, Department of Biological Sciences, University of Southern California, Los Angeles, California, USA

Abstract

The DNA-binding protein from starved cells, Dps, is a universally conserved prokaryotic ferritin that, in many species, also binds DNA. Dps homologs have been identified in the vast majority of bacterial species and several archaea.

Funder

DOD | USAF | AMC | Air Force Office of Scientific Research

HHS | National Institutes of Health

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/jb.00036-22

Reference206 articles.

1. A novel DNA-binding protein with regulatory and protective roles in starved Escherichia coli.

2. Bimodal Protection of DNA by Mycobacterium smegmatis DNA-binding Protein from Stationary Phase Cells

3. Characterization of the sigma 38-dependent expression of a core Escherichia coli starvation gene, pexB

4. The DpsA Protein of Synechococcus sp. Strain PCC7942 Is a DNA-binding Hemoprotein

5. Dps-like proteins: structural and functional insights into a versatile protein family

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