RNase R

Source: Wikipedia, the free encyclopedia.

RNase R, or Ribonuclease R, is a 3'-->5'

mRNA degradation, particularly of non stop mRNAs in bacteria.[1][2] RNase R has homologues
in many other organisms.

When a part of another larger protein has a domain that is very similar to RNase R, this is called an RNase R domain.

Role in trans-translation and ribosomal quality control

RNase R ensures translation accuracy, correct rRNA maturation and elimination of abnormal rRNAs, and is employed by the trans-translation system to break down damaged mRNAs.[3]

In Escherichia coli, RNase R is a 92 kD protein, with the characteristic capacity to degrade structured RNA substrates without displaying sequence specificity. Therefore, RNase R acts over a range of substrates, such as, ribosomal, transfer, messenger and small non-coding RNAs. RNase R is associated with ribonucleoprotein complex that contains tmRNA and SmpB, and is involved in the development of tmRNA under cold-shock.[3]

RNase R is also associated with ribosomes and participates in rRNA, or ribosomal RNA, quality control processes. RNase R has an in vitro affinity for rRNA. In several rRNA quality control pathways, RNase R behaves as a mainfactor by enhancing the removal of faulty rRNA molecules. This protein is also critical for handling rRNA precursors and for observing the ribosome integrity.[3]

RNA digestion

RNase R has two cold shock domains, an RNase catalytic domain, an S1 domain and a basic domain.[4]

Overabundance of RNase R in a cell are harmful since RNase R is more active and more effective in breaking down RNAs than the other bacterial exoribonucleases, such as

RNase II.[5] Besides the substrate RNAs that construct double-stranded RNA with 3' overhangs shorter than seven nucleotides, RNase R can degrade all linear RNAs.[6] For the methodical digestion of eukaryotic linear RNAs, RNase R is a good 3' to 5' exoribonuclease but there are infrequent cases of RNase R resistance. Since mRNAs are not chemically protected at their 3' ends, unlike the protection provided at their 5' ends by the cap structure, RNase R successfully degrades linear mRNAs from their unprotected 3' ends.[4]

References