Open AccessStructural insights into cell cycle control by essential GTPase Era
Author(s) -
Xinhua Ji
Publication year - 2016
Publication title -
postępy biochemii
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.244
H-Index - 15
ISSN - 0032-5422
DOI - 10.18388/pb.2016_33
Subject(s) - ribosome , ribosomal rna , 30s , gtp' , rna , ribosomal protein , 5.8s ribosomal rna , protein subunit , biology , gtpase , eukaryotic small ribosomal subunit , microbiology and biotechnology , biochemistry , chemistry , gene , enzyme
Era (Escherichia coli Ras-like protein), essential for bacterial cell viability, is composed of an N-terminal GTPase domain and a C-terminal KH domain. In bacteria, it is required for the processing of 16S ribosomal RNA (rRNA) and maturation of 30S (small) ribosomal subunit. Era recognizes 10 nucleotides (1530GAUCACCUCC1539) near the 3â end of 16S rRNA and interacts with helix 45 (h45, nucleotides 1506-1529). GTP binding enables Era to bind RNA, RNA binding stimulates Eraâs GTP-hydrolyzing activity, and GTP hydrolysis releases Era from matured 30S ribosomal subunit. As such, Era controls cell growth rate via regulating the maturation of the 30S ribosomal subunit. Ribosomes manufacture proteins in all living organisms. The GAUCA sequence and h45 are highly conserved in all three kingdoms of life. Homologues of Era are present in eukaryotic cells. Hence, the mechanism of bacterial Era action also sheds light on the cell cycle control of eukaryotes.