Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein

Authors

Narayan Iyer
Michael S. Reagan, College of Saint Benedict/Saint John's UniversityFollow
Kou-Juey Wu
Bertram Canagarajah
Errol C. Friedberg

Document Type

Article

Publication Date

2-20-1996

Disciplines

Biochemistry | Biology | Molecular Biology | Molecular Genetics

Abstract

The human basal transcription factor TFIIH plays a central role in two distinct processes. TFIIH is an obligatory component of the RNA polymerase II (RNAP II) transcription initiation complex. Additionally, it is believed to be the core structure around which some if not all the components of the nucleotide excision repair (NER) machinery assemble to constitute a nucleotide excision repairosome. At least two of the subunits of TFIIH (XPB and XPD proteins) are implicated in the disease xeroderma pigmentosum (XP). We have exploited the availability of the cloned XPB, XPD, p62, p44, and p34 genes (all of which encode polypeptide subunits of TFIIH) to examine interactions between in vitro-translated polypeptides by co-immunoprecipitation. Additionally we have examined interactions between TFIIH components, the human NER protein XPG, and the CSB protein which is implicated in Cockayne syndrome (CS). Our analyses demonstrate that the XPB, XPD, p44, and p62 proteins interact with each other. XPG protein interacts with multiple subunits of TFIIH and with CSB protein.

Comments

DOI: 10.1021/bi9524124

Copyright Statement

Reprinted with permission from Biochemistry 35(7): 2157-2167. Copyright 1996 American Chemical Society.

Recommended Citation

Iyer N, Reagan MS, Wu K-J, Canagarajah B, Friedberg EC. 1996. Interactions involving the human RNA polymerase II transcription/nucleotide excision repair complex TFIIH, the nucleotide excision repair protein XPG, and Cockayne syndrome group B (CSB) protein. Biochemistry 35(7): 2157-2167.