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Chemical synthesis of the third WW domain of TCERG 1 by native chemical ligation
Author(s) -
Fidan Zerrin,
Younis Aylin,
Schmieder Peter,
Volkmer Rudolf
Publication year - 2011
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1383
Subject(s) - ww domain , native chemical ligation , rna polymerase ii , rna splicing , chemistry , rna , transcription (linguistics) , stereochemistry , biophysics , biology , biochemistry , computational biology , microbiology and biotechnology , chemical synthesis , gene expression , promoter , in vitro , gene , linguistics , philosophy
The human transcription elongation regulator 1 (TCERG1), with its modular architecture of 3 WW and 6 FF domains, inhibits RNA polymerase II elongation through these WW and FF domains, and interacts with pre‐mRNA splicing factors such as SF1, U2 snRNP and U2AF. WW domains are known as the smallest naturally occurring, monomeric, triple stranded, anti‐parallel β‐sheet structures, generally spanning only about 40 amino acids. The first and second WW domains of TCERG1 have been synthesized and successfully applied for screening cellular targets. In contrast, until now syntheses of the third WW domain yielded oligopeptides with an undefined fold, proving useless for screening cellular targets. This implied that sequence elongation to include the α‐helical structure is crucial for proper folding. We describe here the chemical synthesis of such a 53 residue long TCERG1 WW‐3 domain sequence that exhibits the typical WW domain fold, and could be useful for discovering cellular targets. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.