Ontology highlight
ABSTRACT:
SUBMITTER: Ameres SL
PROVIDER: S-EPMC1920258 | biostudies-literature | 2007
REPOSITORIES: biostudies-literature
Ameres Stefan L SL Shcherbakov Dmitry D Nikonova Ekaterina E Piendl Wolfgang W Schroeder Renée R Semrad Katharina K
Nucleic acids research 20070521 11
RNA chaperone activity is defined as the ability of proteins to either prevent RNA from misfolding or to open up misfolded RNA conformations. One-third of all large ribosomal subunit proteins from E. coli display this activity, with L1 exhibiting one of the highest activities. Here, we demonstrate via the use of in vitro trans- and cis-splicing assays that the RNA chaperone activity of L1 is conserved in all three domains of life. However, thermophilic archaeal L1 proteins do not display RNA cha ...[more]