Reevaluation of the determinants of tyrosine sulfation |
| |
Authors: | Nicholas H B Chan S S Rosenquist G L |
| |
Institution: | (1) Pittsburgh Supercomputing Center, Pittsburgh, PA;(2) Hahnemann University School of Medicine, Philadelphia, PA;(3) Section of Neurobiology, Physiology and Behavior, University of California, One Shields Avenue, 95616 Davis, CA |
| |
Abstract: | The posttranslational sulfation of tyrosine has been though to be initiated by the recognition of specific consensus features
by the sulfating enzyme tyrosylprotein sulfotransferase (TPST). However, using these recognition features to identify new
tyrosine sulfation sites misses recently characterized sites that lack these features. Rigorous analysis of the amino acids
surrounding the target tyrosin using the position-specific scoring matrix (PSSM) demonstrates that a consensus sequence does
not contain all the information necessary to predict tyrosine sulfation. Instead, accurate prediction requires consideration
of all residues within five amino acids on either side of the target tyrosine. These results support the notion that secondary
structure is the major determinant of sulfation and that other residues within the sulfation site can compensate for deviations
from commonly observed features. This view implies that specific consensus features are not critical for TPST substrate recognition
but that TPST may instead broadly recognize any sufficiently exposed tyrosine residue. |
| |
Keywords: | Tyrosine sulfation posttranslational processing tyrosyl protein sulfotransferase |
本文献已被 PubMed SpringerLink 等数据库收录! |
|