Data Entry: Please note that the research database will be replaced by UNIverse by the end of October 2023. Please enter your data into the system https://universe-intern.unibas.ch. Thanks

Login for users with Unibas email account...

Login for registered users without Unibas email account...

 
A unique Extradenticle recruitment mode in the Drosophila Hox protein Ultrabithorax
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 155910
Author(s) Merabet, Samir; Saadaoui, Mehdi; Sambrani, Nagraj; Hudry, Bruno; Pradel, Jacques; Affolter, Markus; Graba, Yacine
Author(s) at UniBasel Affolter, Markus
Year 2007
Title A unique Extradenticle recruitment mode in the Drosophila Hox protein Ultrabithorax
Journal Proceedings of the National Academy of Sciences of the United States of America
Volume 104
Number 43
Pages / Article-Number 16946-51
Keywords development, transcription, hexapeptide, UbdA
Abstract

Hox transcription factors are essential for shaping body morphology in development and evolution. The control of Hox protein activity in part arises from interaction with the PBC class of partners, pre-B cell transcription factor (Pbx) proteins in vertebrates and Extradenticle (Exd) in Drosophila. Characterized interactions occur through a single mode, involving a short hexapeptide motif in the Hox protein. This apparent uniqueness in Hox-PBC interaction provides little mechanistic insight in how the same cofactors endow Hox proteins with specific and diverse activities. Here, we identify in the Drosophila Ultrabithorax (Ubx) protein a short motif responsible for an alternative mode of Exd recruitment. Together with previous reports, this finding highlights that the Hox protein Ubx has multiple ways to interact with the Exd cofactor and suggests that flexibility in Hox-PBC contacts contributes to specify and diversify Hox protein function.

Publisher National Academy of Sciences
ISSN/ISBN 0027-8424
edoc-URL http://edoc.unibas.ch/dok/A5258906
Full Text on edoc No
Digital Object Identifier DOI 10.1073/pnas.0705832104
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/17942685
ISI-Number WOS:000250487600041
Document type (ISI) Journal Article
 
   

MCSS v5.8 PRO. 0.336 sec, queries - 0.000 sec ©Universität Basel  |  Impressum   |    
29/03/2024