A human protein with homology to Saccharomyces cerevisiae SNF5 interacts with the potential helicase hbrm (original) (raw)

Journal Article

,

Search for other works by this author on:

,

1

Whitehead institute for Biomedical Research

9 Cambridge Center, Cambridge, MA 02142, USA

Search for other works by this author on:

,

Search for other works by this author on:

,

1

Whitehead institute for Biomedical Research

9 Cambridge Center, Cambridge, MA 02142, USA

Search for other works by this author on:

* To whom correspondence should be addressed

Search for other works by this author on:

Received:

23 January 1995

Revision received:

17 February 1995

Accepted:

17 February 1995

Cite

Christian Muchardt, Claude Sardet, Brigitte Bourachot, Christina Onufryk, Moshe Yaniv, A human protein with homology to Saccharomyces cerevisiae SNF5 interacts with the potential helicase hbrm , Nucleic Acids Research, Volume 23, Issue 7, 11 April 1995, Pages 1127–1132, https://doi.org/10.1093/nar/23.7.1127
Close

Navbar Search Filter Mobile Enter search term Search

Abstract

ABSTRACT

In yeast, the SNF/SWI complex is involved in transcriptional activation of several inducible promoters, possiblyby causing a local modification of the chromatin structure. Recently, two human homologues of the SNF2/SWI2 proteinhave been isolated, hbrm and BAG-1. In addition, a complex containing one of the SNF2/SWI2 homologues and having an In vitro activity similar to the yeast complex has been partially purified from HeLa cells. Here we describe the characterization of a cDNA encoding a human nuclear protein containing a large domain of homology with SNF5, another member of the yeast SNF/SW1 complex. This protein can be co-immunoprecipitated with hbrm and the interaction between the two proteins is dependent on the region conserved between the human and the yeast SNF5. These findings suggest that the cDNA we have cloned encodes one of the members of the human SNF/SWI complex.

This content is only available as a PDF.

© 1995 Oxford University Press

I agree to the terms and conditions. You must accept the terms and conditions.

Submit a comment

Name

Affiliations

Comment title

Comment

You have entered an invalid code

Thank you for submitting a comment on this article. Your comment will be reviewed and published at the journal's discretion. Please check for further notifications by email.

Citations

Views

Altmetric

Metrics

Total Views 84

32 Pageviews

52 PDF Downloads

Since 2/1/2017

Month: Total Views:
February 2017 1
June 2017 4
July 2017 2
August 2017 1
September 2017 1
October 2017 1
November 2017 1
December 2017 5
January 2018 3
February 2018 11
March 2018 9
April 2018 14
June 2018 1
July 2018 1
July 2019 2
August 2019 1
October 2019 2
October 2020 1
January 2021 1
October 2022 1
November 2022 1
December 2022 1
January 2023 1
May 2023 2
September 2023 2
November 2023 1
March 2024 1
April 2024 3
June 2024 3
July 2024 2
August 2024 1
September 2024 1
October 2024 2

Citations

119 Web of Science

×

Email alerts

Citing articles via

More from Oxford Academic