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

exoribonuclease An exoribonuclease is an exonuclease ribonuclease, which are enzymes that degrade RNA by removing terminal nucleotides from either the 5' end or the 3' end of the RNA molecule. Enzymes that remove nucleotides from the 5' end are called ''5'-3 ...

, which belongs to the RNase II superfamily, a group of enzymes that hydrolyze RNA in the 3' - 5' direction. RNase R has been shown to be involved in selective

mRNA In molecular biology, messenger ribonucleic acid (mRNA) is a single-stranded molecule of RNA that corresponds to the genetic sequence of a gene, and is read by a ribosome in the process of synthesizing a protein. mRNA is created during the ...

degradation, particularly of non stop mRNAs in bacteria. 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 Ribosomal ribonucleic acid (rRNA) is a type of non-coding RNA which is the primary component of ribosomes, essential to all cells. rRNA is a ribozyme which carries out protein synthesis in ribosomes. Ribosomal RNA is transcribed from ribosoma ...

maturation and elimination of abnormal rRNAs, and is employed by the ''trans''-translation system to break down damaged mRNAs. In ''

Escherichia coli ''Escherichia coli'' (),Wells, J. C. (2000) Longman Pronunciation Dictionary. Harlow ngland Pearson Education Ltd. also known as ''E. coli'' (), is a Gram-negative, facultative anaerobic, rod-shaped, coliform bacterium of the genus '' Esc ...

,'' 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. RNase R is also associated with ribosomes and participates in

, or ribosomal RNA, quality control processes. RNase R has an ''

in vitro ''In vitro'' (meaning in glass, or ''in the glass'') studies are performed with microorganisms, cells, or biological molecules outside their normal biological context. Colloquially called " test-tube experiments", these studies in biology ...

'' 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.

RNA digestion

RNase R has two cold shock domains, an RNase catalytic domain, an S1 domain and a basic domain. 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. Besides the substrate RNAs that construct double-stranded RNA with 3' overhangs shorter than seven nucleotides, RNase R can degrade all linear RNAs. 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.

References

Ribonucleases {{enzyme-stub