An atypical heterotrimeric Gα protein has substantially reduced nucleotide binding but retains nucleotide-independent interactions with its cognate RGS protein and Gβγ dimer.
AGB1
Arabidopsis
AtGPA1
AtRGS1
Gβγ
XLG2
dominant negative G alpha
extra-large G protein
Journal
Journal of biomolecular structure & dynamics
ISSN: 1538-0254
Titre abrégé: J Biomol Struct Dyn
Pays: England
ID NLM: 8404176
Informations de publication
Date de publication:
Oct 2020
Oct 2020
Historique:
pubmed:
17
12
2019
medline:
22
6
2021
entrez:
17
12
2019
Statut:
ppublish
Résumé
Plants uniquely have a family of proteins called extra-large G proteins (XLG) that share homology in their C-terminal half with the canonical Gα subunits; we carefully detail here that Arabidopsis XLG2 lacks critical residues requisite for nucleotide binding and hydrolysis which is consistent with our quantitative analyses. Based on microscale thermophoresis, Arabidopsis XLG2 binds GTPγS with an affinity 100 times lower than that to canonical Gα subunits. This means that given the concentration range of guanine nucleotide in plant cells, XLG2 is not likely bound by GTP
Identifiants
pubmed: 31838952
doi: 10.1080/07391102.2019.1704879
pmc: PMC7308192
mid: NIHMS1547727
doi:
Substances chimiques
Arabidopsis Proteins
0
Nucleotides
0
RGS Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
5204-5218Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM065989
Pays : United States
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