Identification of GroEL as a constituent of an mRNA-protection complex in Escherichia coli.
An RNA-binding activity has been identified in Escherichia coli that provides physical protection of RNA against ribonucleases in an ATP- and Mg(2+)-dependent manner. This binding activity is stimulated under growth conditions known to cause a decrease in the rate of mRNA decay. RNA protection is mediated by a protein complex that contains a modified form of the chaperonin GroEL as an indispensable constituent. These results suggest a new role for GroEL as an RNA chaperone.
Georgellis
D
D
Institute of Microbiology and Genetics, Vienna Biocenter, Austria.
Sohlberg
B
B
Hartl
F U
FU
von Gabain
A
A
D000244:Adenosine Diphosphate / Q000494:pharmacology; D000255:Adenosine Triphosphate / Q000494:pharmacology; D000911:Antibodies, Monoclonal / Q000276:immunology; D015153:Blotting, Western; D018834:Chaperonin 60 / Q000302:isolation & purification / Q000378:metabolism*; D003570:Cytidine Triphosphate / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism*; D018832:Molecular Chaperones / Q000378:metabolism*; D017510:Protein Folding; D012333:RNA, Messenger / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000378:metabolism*; D012260:Ribonucleases / Q000378:metabolism
D000911:Antibodies, Monoclonal; D018834:Chaperonin 60; D018832:Molecular Chaperones; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D000244:Adenosine Diphosphate; D003570:Cytidine Triphosphate; D000255:Adenosine Triphosphate; D012260:Ribonucleases