Dual specificity of a prokaryotic GTPase-activating protein (GAP) to two small Ras-like GTPases in Myxococcus xanthus.
Amino Acid Sequence
Bacterial Proteins
/ chemistry
Binding Sites
Cell Polarity
Cloning, Molecular
Escherichia coli
/ genetics
Fimbriae, Bacterial
/ genetics
GTP Phosphohydrolases
/ chemistry
GTPase-Activating Proteins
/ chemistry
Gene Expression
Genetic Vectors
/ chemistry
Guanine Nucleotide Exchange Factors
/ chemistry
Guanosine Diphosphate
/ chemistry
Guanosine Triphosphate
/ chemistry
Hydrolysis
Kinetics
Models, Molecular
Myxococcus xanthus
/ genetics
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
Protein Isoforms
/ chemistry
Recombinant Proteins
/ chemistry
Sequence Alignment
Sequence Homology, Amino Acid
GTPase-activating protein
MglA
MglB
SofG
dual specificity
small Ras-like GTPase
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
03 2021
03 2021
Historique:
received:
12
11
2019
revised:
22
06
2020
accepted:
28
07
2020
pubmed:
11
8
2020
medline:
21
7
2021
entrez:
11
8
2020
Statut:
ppublish
Résumé
Two small Ras-like GTPases, MglA and SofG, work in synchrony to drive cell polarity and motility in the soil bacterium, Myxococcus xanthus. While MglA regulates two types of motility in Myxococcus and drives cell polarity reversals, SofG regulates social motility enabled by the type IV pili (T4P) machinery. In order to understand the molecular basis of how multiple GTPases act concertedly, we initiated biochemical studies on SofG. A construct of SofG (SofG
Substances chimiques
Bacterial Proteins
0
GTPase-Activating Proteins
0
Guanine Nucleotide Exchange Factors
0
Protein Isoforms
0
Recombinant Proteins
0
Guanosine Diphosphate
146-91-8
Guanosine Triphosphate
86-01-1
GTP Phosphohydrolases
EC 3.6.1.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1565-1585Informations de copyright
© 2020 Federation of European Biochemical Societies.
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