The archaic chaperone–usher pathways may depend on donor strand exchange for intersubunit interactions
Author:
Affiliation:
1. Key Laboratory of Ministry of Education for Developmental Genes and Human Diseases, Southeast University, Nanjing, Jiangsu 210009, PR China
2. Department of Biochemistry, Southeast University School of Medicine, Nanjing, Jiangsu 210009, PR China
Abstract
Funder
Natural Science Foundation of China
Publisher
Microbiology Society
Subject
Microbiology
Reference31 articles.
1. PapD-like chaperones provide the missing information for folding of pilin proteins
2. Development of pilus organelle subassemblies in vitro depends on chaperone uncapping of a beta zipper
3. X-ray Structure of the FimC-FimH Chaperone-Adhesin Complex from Uropathogenic Escherichia coli
4. Identification of Major Sporulation Proteins of Myxococcus xanthus Using a Proteomic Approach
5. Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria
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1. Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information;Journal of Biological Chemistry;2018-11
2. Molecular Mechanisms of Signaling in Myxococcus xanthus Development;Journal of Molecular Biology;2016-09
3. A gene encoding a potential adenosine 5′-phosphosulphate kinase is necessary for timely development of Myxococcus xanthus;Microbiology;2016-04-01
4. Identification of a Putative Flavin Adenine Dinucleotide-Binding Monooxygenase as a Regulator for Myxococcus xanthus Development;Journal of Bacteriology;2015-01-20
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