Dph7 catalyzes a previously unknown demethylation step in diphthamide biosynthesis.

ABSTRACT: Present on archaeal and eukaryotic translation elongation factor 2, diphthamide represents one of the most intriguing post-translational modifications on proteins. The biosynthesis of diphthamide was proposed to occur in three steps requiring seven proteins, Dph1-7, in eukaryotes. The functional assignments of Dph1-5 in the first and second step have been well established. Recent studies suggest that Dph6 (yeast YLR143W or human ATPBD4) and Dph7 (yeast YBR246W or human WDR85) are involved in the last amidation step, with Dph6 being the actual diphthamide synthetase catalyzing the ATP-dependent amidation reaction. However, the exact molecular role of Dph7 is unclear. Here we demonstrate that Dph7 is an enzyme catalyzing a previously unknown step in the diphthamide biosynthesis pathway. This

SUBMITTER: Lin Z 

PROVIDER: S-EPMC4015618 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature