RNase PH

RNase PH is an 3'-5' exoribonuclease and nucleotidyltransferase, present in archaea and bacteria, that is involved in tRNA processing. Contrary to hydrolytic enzymes, it is a phosphorolytic enzyme, meaning that it uses inorganic phosphate as a cofactor to cleave nucleotide-nucleotide bonds, releasing diphosphate nucleotides. The active structure of the proteins is actually a homohexameric complex, consisting of three RNase PH dimers. [1] RNase PH has homologues in many other organisms, which are referred to as RNase PH-like proteins. When a part of another larger protein has a domain that is very similar to RNase PH, this is called an RNase PH domain (RPD).

See also

Two highly related exoribonuclease complexes:

* Polynucleotide phosphorylase
* Exosome complex

References

1. ^ Ishii et al.; Nureki, O; Yokoyama, S (2003). "Crystal structure of the tRNA processing enzyme RNase PH from Aquifex aeolicus". J Biol Chem. 278 (34): 32397–404. doi:10.1074/jbc.M300639200. PMID 12746447.

External links

* Crystal structure of Aquifex aeolicus RNase PH at the RCSB Protein Data Bank

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