Abstract:
:Tissue transglutaminase (TG2) catalyzes the Ca(2+)-dependent posttranslational modification of proteins via formation of isopeptide bonds between their glutamine and lysine residues. Although substrate specificity of TG2 has been studied repeatedly at the sequence level, no clear consensus sequences have been determined so far. With the use of the extensive structural information on TG2 substrate proteins listed in TRANSDAB Wiki database, a slight preference of TG2 for glutamine and lysine residues situated in turns could be observed. When the spatial environment of the favored glutamine and lysine residues was analyzed with logistic regression, the presence of specific amino acid patterns was identified. By using the occurrence of the predictor amino acids as selection criteria, several polypeptides were predicted and later identified as novel in vitro substrates for TG2. By studying the sequence of TG2 substrate proteins lacking available crystal structure, the strong favorable influence on substrate selection of the presence of substrate glutamine and lysine residues in intrinsically disordered regions could also be revealed. The collected structural data have provided novel understanding of how this versatile enzyme selects its substrates in various cell compartments and tissues.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Csosz E,Bagossi P,Nagy Z,Dosztanyi Z,Simon I,Fesus Ldoi
10.1016/j.jmb.2008.08.026subject
Has Abstractpub_date
2008-11-07 00:00:00pages
390-402issue
2eissn
0022-2836issn
1089-8638pii
S0022-2836(08)01019-Xjournal_volume
383pub_type
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