title: It takes two to rule translation elongation.
abstract: In this issue of Structure, Glatt and colleagues report the structure of the Kti11/Kti13 heterodimer. This study reveals how dimerization and Fe(2+) binding are required for modification of both tRNA and EF2, thus suggesting a mechanism for regulation of translation elongation via two different pathways.
authors.affiliation: Structural Biology Brussels, Vrije Universiteit Brussel (VUB), 1050 Brussels, Belgium; Structural Biology Research Center, VIB, 1050 Brussels, Belgium. Electronic address: wim.versees@vib-vub.be.
authors.forename: Wim
authors.initials: W
authors.lastname: Versées
mesh_terms: D020652:Peptide Elongation Factor 2 / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism*; D012097:Repressor Proteins / Q000737:chemistry* / Q000502:physiology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000502:physiology*
chemical_list: D020652:Peptide Elongation Factor 2; D012097:Repressor Proteins; D029701:Saccharomyces cerevisiae Proteins; D012343:RNA, Transfer