The Histone H1-Like Protein AlgP Facilitates Even Spacing of Polyphosphate Granules in Pseudomonas aeruginosa
Author:
Affiliation:
1. Department of Integrative Structural and Computational Biology, Scripps Research, La Jolla, California, USA
2. Department of Immunology and Microbiology, Scripps Research, La Jolla, California, USA
Abstract
Funder
Donald E. and Delia B. Baxter Foundation
HHS | NIH | National Institute of General Medical Sciences
Scripps Research
Publisher
American Society for Microbiology
Subject
Virology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/mbio.02463-21
Reference70 articles.
1. Inorganic Polyphosphate: Essential for Growth and Survival
2. Model systems for studying polyphosphate biology: a focus on microorganisms
3. Enzymes of Inorganic Polyphosphate Metabolism
4. Proteins with CHADs (Conserved Histidine α-Helical Domains) Are Attached to Polyphosphate Granules In Vivo and Constitute a Novel Family of Polyphosphate-Associated Proteins (Phosins)
5. Molecular characterization of CHAD domains as inorganic polyphosphate-binding modules
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