RNA chaperone activity of large ribosomal subunit proteins from Escherichia coli.
The ribosome is a highly dynamic ribonucleoprotein machine. During assembly and during translation the ribosomal RNAs must routinely be prevented from falling into kinetic folding traps. Stable occupation of these trapped states may be prevented by proteins with RNA chaperone activity. Here, ribosomal proteins from the large (50S) ribosome subunit of Escherichia coli were tested for RNA chaperone activity in an in vitro trans splicing assay. Nearly a third of the 34 large ribosomal subunit proteins displayed RNA chaperone activity. We discuss a possible role of this function during ribosome assembly and during translation.
Semrad
Katharina
K
Max F Perutz Laboratories, Institute of Microbiology and Genetics, Dr. Bohrgasse 9/4, 1030 Vienna, Austria. katharina.semrad@univie.ac.at
Green
Rachel
R
Schroeder
Renée
R
D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D007700:Kinetics; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D014176:Protein Biosynthesis; D012326:RNA Splicing; D012329:RNA, Bacterial / Q000235:genetics / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*; D012270:Ribosomes / Q000235:genetics / Q000378:metabolism
D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; D012329:RNA, Bacterial; D012269:Ribosomal Proteins