Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form

RNA-dependent cysteine biosynthesis in archaea

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Sauerwald, A.
  • Zhu, W. H.
  • Major, T. A.
  • Roy, H.
  • Palioura, S.
  • Jahn, D.
  • Whitman, W. B.
  • Yates III, John
  • Ibba, M.
  • Soll, D.

publication date

  • March 2005

journal

  • Science  Journal

abstract

  • Several methanogenic archaea lack cysteinyl-transfer RNA (tRNA) synthetase (CysRS), the essential enzyme that provides Cys-tRNA(Cys) for translation in most organisms. Partial purification of the corresponding activity from Methanocaldococcus jannaschii indicated that tRNA(Cys) becomes acylated with O-phosphoserine (Sep) but not with cysteine. Further analyses identified a class II-type O-phosphoseryl-tRNA synthetase (SepRS) and Sep-tRNA:Cys-tRNA synthase (SepCysS). SepRS specifically forms Sep-tRNA(Cys), which is then converted to Cys-tRNA(Cys) by SepCysS. Comparative genomic analyses suggest that this pathway, encoded in all organisms lacking CysRS, can also act as the sole route for cysteine biosynthesis. This was proven for Methanococcus maripaludis, where deletion of the SepRS-encoding gene resulted in cysteine auxotrophy. As the conversions of Sep-tRNA to Cys-tRNA or to selenocysteinyl-tRNA are chemically analogous, the catalytic activity of SepCysS provides a means by which both cysteine and selenocysteine may have originally been added to the genetic code.

subject areas

  • Adenosine Triphosphate
  • Amino Acyl-tRNA Synthetases
  • Archaea
  • Cysteine
  • Methanococcales
  • Methanococcus
  • Oxidation-Reduction
  • Phosphoserine
  • RNA, Archaeal
  • RNA, Transfer, Amino Acyl
  • RNA, Transfer, Cys
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1108329

PubMed ID

  • 15790858
scroll to property group menus

Additional Document Info

start page

  • 1969

end page

  • 1972

volume

  • 307

issue

  • 5717

©2021 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support