Poly(A)-specific ribonuclease (PARN): An allosterically regulated, processive and mRNA cap-interacting deadenylase

Poly(A)-specific ribonuclease (PARN) : An allosterically regulated, processive and mRNA cap-interacting deadenylase

Deadenylation of eukaryotic mRNA is a mechanism critical for mRNA function by influencing mRNA turnover and efficiency of protein synthesis. Here, we review poly(A)-specific ribonuclease (PARN), which is one of the biochemically best characterized deadenylases. PARN is unique among the currently known eukaryotic poly(A) degrading nucleases, being the only deadenylase that has the capacity to directly interact during poly(A) hydrolysis with both the m 7 G-cap structure and the poly(A) tail of the mRNA. In short, PARN is a divalent metal-ion dependent poly(A)-specific, processive and cap-interacting 3'-5' exoribonuclease that efficiently degrades poly(A) tails of eukaryotic mRNAs. We discuss in detail the mechanisms of its substrate recognition, catalysis, allostery and processive mode of action. On the basis of biochemical and structural evidence, we present and discuss a working model for PARN action. Models of regulation of PARN activity by trans-acting factors are discussed as well as the physiological relevance of PARN.

Henriksson, NiklasUppsala universitet,Kemisk biologi (författare)
Nilsson, PerUppsala universitet,Kemisk biologi (författare)
Nissbeck, MikaelUppsala universitet,Kemisk biologi(Swepub:uu)mikni841 (författare)
Uppsala universitetKemisk biologi (creator_code:org_t)

Ingår i:Critical reviews in biochemistry and molecular biology: Informa UK Limited48:2, s. 192-2091040-92381549-7798

Av författaren/redakt...: Virtanen, Anders; Henriksson, Nikl ...; Nilsson, Per; Nissbeck, Mikael

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.