Premium
Structural insight into the interaction of ADP‐ribose with the PARP WWE domains
Author(s) -
He Fahu,
Tsuda Kengo,
Takahashi Mari,
Kuwasako Kanako,
Terada Takaho,
Shirouzu Mikako,
Watanabe Satoru,
Kigawa Takanori,
Kobayashi Naohiro,
Güntert Peter,
Yokoyama Shigeyuki,
Muto Yutaka
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.09.009
Subject(s) - poly adp ribose polymerase , ribose , ubiquitin , chemistry , biochemistry , domain (mathematical analysis) , dna repair , polymerase , stereochemistry , dna , computational biology , microbiology and biotechnology , biophysics , biology , enzyme , mathematical analysis , mathematics , gene
The WWE domain is often identified in proteins associated with ubiquitination or poly‐ADP‐ribosylation. Structural information about WWE domains has been obtained for the ubiquitination‐related proteins, such as Deltex and RNF146, but not yet for the poly‐ADP‐ribose polymerases (PARPs). Here we determined the solution structures of the WWE domains from PARP11 and PARP14, and compared them with that of the RNF146 WWE domain. NMR perturbation experiments revealed the specific differences in their ADP‐ribose recognition modes that correlated with their individual biological activities. The present structural information sheds light on the ADP‐ribose recognition modes by the PARP WWE domains.