Isolation and expression pattern of RGS21 gene, a novel RGS member.
Author(s) -
Xin Li,
Lei Chen,
Chaoneng Ji,
Bing Liu,
Jiefeng Gu,
Jian Xu,
Xianqiong Zou,
Shaohua Gu,
Yumin Mao
Publication year - 2005
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.2005_3412
Subject(s) - gtpase activating protein , rgs2 , subfamily , complementary dna , biology , gene , regulator of g protein signaling , gtpase , g protein , genetics , gene family , protein family , cdna library , messenger rna , microbiology and biotechnology , gene expression , signal transduction
Regulators of G-protein signaling (RGS) proteins are known for the RGS domain that is composed of a conserved stretch of 120 amino acids, which binds directly to activated G-protein alpha subunits and acts as a GTPase-activating protein (GAP), leading to their deactivation and termination of downstream signals. In this study, a novel human RGS cDNA (RGS21), 1795 bp long and encoding a 152-amino acid polypeptide, was isolated by large-scale sequencing analysis of a human fetal brain cDNA library. Unlike other RGS family members, RGS21 gene has no additional domain/motif and may represent the smallest known member of RGS family. It may belong to the B/R4 subfamily, which suggests that it may serve exclusively as a negative regulator of alphai/o family members and/or alphaq/11. PCR analysis showed that RGS21 mRNA was expressed ubiquitously in the 16 tissues examined, implying general physiological roles.
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