Structural conservation of the PIN domain active site across all domains of life

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

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  • M Senissar, Centre for Bacterial Stress Response and Persistence, Department of Molecular Biology and Genetics, Aarhus University, Gustav Wieds Vej 10c, 8000, Aarhus C, Denmark. deb@mbg.au.dk.
  • ,
  • M C Manav
  • D E Brodersen

The PIN domain (Pil N-terminus) is a compact RNA-binding protein domain present in all domains of life. This 120-residue domain consists of a central and parallel β sheet surrounded by α helices, which together organise 4-5 acidic residues in an active site that binds one or more divalent metal ions and in many cases has endoribonuclease activity. In bacteria and archaea, the PIN domain is primarily associated with toxin-antitoxin loci, consisting of a toxin (the PIN domain nuclease) and an antitoxin that inhibits the function of the toxin under normal growth conditions. During nutritional or antibiotic stress, the antitoxin is proteolytically degraded causing activation of the PIN domain toxin leading to a dramatic reprogramming of cellular metabolism to cope with the new conditions. In eukaryotes, PIN domains are commonly found as parts of larger proteins and are involved in a range of processes involving RNA cleavage, including ribosomal RNA biogenesis and nonsense-mediated mRNA decay. In this review, we provide a comprehensive overview of the structural characteristics of the PIN domain and compare PIN domains from all domains of life in terms of structure, active site architecture, and activity. This article is protected by copyright. All rights reserved.

OriginalsprogEngelsk
TidsskriftProtein Science
Vol/bind26
Nummer8
Sider (fra-til)1474-1492
Antal sider19
ISSN0961-8368
DOI
StatusUdgivet - 2017

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