English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The bifunctional protein DCoH modulates interactions of the homeodomain transcription factor HNF1 with nucleic acids

Rhee, K., Stier, G., Becker, P. B., Suck, D., & Sandaltzopoulos, R. (1997). The bifunctional protein DCoH modulates interactions of the homeodomain transcription factor HNF1 with nucleic acids. Journal of Molecular Biology (London), 265(1), 20-29. doi:10.1006/jmbi.1996.0708.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A60F-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-AAF7-6
Genre: Journal Article

Files

show Files
hide Files
:
JMolBiol_265_1997_20.pdf (Any fulltext), 718KB
 
File Permalink:
-
Name:
JMolBiol_265_1997_20.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Creators

show
hide
 Creators:
Rhee, Kyong−Hi, Author
Stier, Gunter1, Author              
Becker, Peter B., Author
Suck, Dietrich, Author
Sandaltzopoulos, Raphael, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: solid-phase footprintin; protein/DNA complex stability; DNA binding; RNA binding; pterin-4a-carbinolamine dehydratase
 Abstract: The hepatocyte nuclear factor-1 (HNF1) is a homeodomain transcription factor that binds DNA as a dimer. HNF1 dimers associate with two molecules of DCoH, a bifunctional protein that also has an enzymatic function in the tetrahydrobiopterin regeneration, to form stable heterotetramers also capable of DNA binding. Employing purified, recombinant HNF1, HNF1/DCoH heterotetramers and DCoH homotetramers we investigated whether DCoH affects interactions of HNF1 with nucleic acids. Although we detected no direct binding of DCoH to DNA or RNA, DCoH stabilized HNF1/DNA complexes and promoted interactions with sub-optimal DNA target sequences such as the human alpha1-antitrypsin TATA box region. Importantly, we also observed interactions of HNF1 with RNA, but these interactions were completely abolished when HNF1 was complexed with DCoH. Interestingly, DCoH retains its enzymatic activity while complexed with HNF1. Our results document intermolecular regulation of HNF1 binding to nucleic acids by DCoH.

Details

show
hide
Language(s): eng - English
 Dates: 1996-10-081996-05-241996-10-082002-05-251997-01-10
 Publication Status: Published in print
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664795
DOI: 10.1006/jmbi.1996.0708
URI: https://www.ncbi.nlm.nih.gov/pubmed/8995521
Other: 7342
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Academic Press
Pages: - Volume / Issue: 265 (1) Sequence Number: - Start / End Page: 20 - 29 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042