The HMG-domain Protein BAP111 is Important for the Function of the BRM Chromatin-remodeling Complex in Vivo

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 2001 May 2

PMID 11331758

Citations 32

Authors

O Papoulas

G Daubresse

J A Armstrong

J Jin

M P Scott

J W Tamkun

Affiliations

Soon will be listed here.

Abstract

The Drosophila trithorax group gene brahma (brm) encodes the ATPase subunit of a SWI/SNF-like chromatin-remodeling complex. A key question about chromatin-remodeling complexes is how they interact with DNA, particularly in the large genomes of higher eukaryotes. Here, we report the characterization of BAP111, a BRM-associated protein that contains a high mobility group (HMG) domain predicted to bind distorted or bent DNA. The presence of an HMG domain in BAP111 suggests that it may modulate interactions between the BRM complex and chromatin. BAP111 is an abundant nuclear protein that is present in all cells throughout development. By using gel filtration chromatography and immunoprecipitation assays, we found that the majority of BAP111 protein in embryos is associated with the BRM complex. Furthermore, heterozygosity for BAP111 enhanced the phenotypes resulting from a partial loss of brm function. These data demonstrate that the BAP111 subunit is important for BRM complex function in vivo.

Citing Articles

Comprehensive identification of SWI/SNF complex subunits underpins deep eukaryotic ancestry and reveals new plant components.

Hernandez-Garcia J, Diego-Martin B, Kuo P, Jami-Alahmadi Y, Vashisht A, Wohlschlegel J Commun Biol. 2022; 5(1):549.

PMID: 35668117 PMC: 9170682. DOI: 10.1038/s42003-022-03490-x.

Capturing the transcription factor interactome in response to sub-lethal insecticide exposure.

Ingham V, Elg S, Nagi S, Dondelinger F Curr Res Insect Sci. 2022; 1:None.

PMID: 34977825 PMC: 8702396. DOI: 10.1016/j.cris.2021.100018.

GBAF, a small BAF sub-complex with big implications: a systematic review.

Innis S, Cabot B Epigenetics Chromatin. 2020; 13(1):48.

PMID: 33143733 PMC: 7607862. DOI: 10.1186/s13072-020-00370-8.

The BAF complex in development and disease.

Alfert A, Moreno N, Kerl K Epigenetics Chromatin. 2019; 12(1):19.

PMID: 30898143 PMC: 6427853. DOI: 10.1186/s13072-019-0264-y.

Pleiotropic effects of regulatory variation in tan result in correlation of two pigmentation traits in Drosophila melanogaster.

Endler L, Gibert J, Nolte V, Schlotterer C Mol Ecol. 2018; .

PMID: 29957826 PMC: 6120501. DOI: 10.1111/mec.14781.

References

Lee C, Murphy M, Lee J, Chung J . Targeting a SWI/SNF-related chromatin remodeling complex to the beta-globin promoter in erythroid cells. Proc Natl Acad Sci U S A. 1999; 96(22):12311-5. PMC: 22913. DOI: 10.1073/pnas.96.22.12311. View

Kent W, Zahler A . The intronerator: exploring introns and alternative splicing in Caenorhabditis elegans. Nucleic Acids Res. 1999; 28(1):91-3. PMC: 102389. DOI: 10.1093/nar/28.1.91. View

Collins R, Furukawa T, Tanese N, Treisman J . Osa associates with the Brahma chromatin remodeling complex and promotes the activation of some target genes. EMBO J. 1999; 18(24):7029-40. PMC: 1171766. DOI: 10.1093/emboj/18.24.7029. View

Kowenz-Leutz E, Leutz A . A C/EBP beta isoform recruits the SWI/SNF complex to activate myeloid genes. Mol Cell. 2000; 4(5):735-43. DOI: 10.1016/s1097-2765(00)80384-6. View

Strahl B, Allis C . The language of covalent histone modifications. Nature. 2000; 403(6765):41-5. DOI: 10.1038/47412. View

Brown C, Lechner T, Howe L, Workman J . The many HATs of transcription coactivators. Trends Biochem Sci. 2000; 25(1):15-9. DOI: 10.1016/s0968-0004(99)01516-9. View

Phelan M, Sif S, Narlikar G, Kingston R . Reconstitution of a core chromatin remodeling complex from SWI/SNF subunits. Mol Cell. 1999; 3(2):247-53. DOI: 10.1016/s1097-2765(00)80315-9. View

Cosma M, Tanaka T, Nasmyth K . Ordered recruitment of transcription and chromatin remodeling factors to a cell cycle- and developmentally regulated promoter. Cell. 1999; 97(3):299-311. DOI: 10.1016/s0092-8674(00)80740-0. View

Bourachot B, Yaniv M, Muchardt C . The activity of mammalian brm/SNF2alpha is dependent on a high-mobility-group protein I/Y-like DNA binding domain. Mol Cell Biol. 1999; 19(6):3931-9. PMC: 104352. DOI: 10.1128/MCB.19.6.3931. View

10.

Krebs J, Kuo M, Allis C, Peterson C . Cell cycle-regulated histone acetylation required for expression of the yeast HO gene. Genes Dev. 1999; 13(11):1412-21. PMC: 316758. DOI: 10.1101/gad.13.11.1412. View

11.

Orphanides G, Wu W, Lane W, Hampsey M, Reinberg D . The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. Nature. 1999; 400(6741):284-8. DOI: 10.1038/22350. View

12.

Kingston R, Narlikar G . ATP-dependent remodeling and acetylation as regulators of chromatin fluidity. Genes Dev. 1999; 13(18):2339-52. DOI: 10.1101/gad.13.18.2339. View

13.

Travers A . Recognition of distorted DNA structures by HMG domains. Curr Opin Struct Biol. 2000; 10(1):102-9. DOI: 10.1016/s0959-440x(99)00056-1. View

14.

Vignali M, Hassan A, Neely K, Workman J . ATP-dependent chromatin-remodeling complexes. Mol Cell Biol. 2000; 20(6):1899-910. PMC: 110808. DOI: 10.1128/MCB.20.6.1899-1910.2000. View

15.

Ng H, Bird A . Histone deacetylases: silencers for hire. Trends Biochem Sci. 2000; 25(3):121-6. DOI: 10.1016/s0968-0004(00)01551-6. View

16.

Kamachi Y, Uchikawa M, Kondoh H . Pairing SOX off: with partners in the regulation of embryonic development. Trends Genet. 2000; 16(4):182-7. DOI: 10.1016/s0168-9525(99)01955-1. View

17.

Sudarsanam P, Iyer V, Brown P, Winston F . Whole-genome expression analysis of snf/swi mutants of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 2000; 97(7):3364-9. PMC: 16245. DOI: 10.1073/pnas.97.7.3364. View

18.

Dallas P, Pacchione S, Wilsker D, Bowrin V, Kobayashi R, Moran E . The human SWI-SNF complex protein p270 is an ARID family member with non-sequence-specific DNA binding activity. Mol Cell Biol. 2000; 20(9):3137-46. PMC: 85608. DOI: 10.1128/MCB.20.9.3137-3146.2000. View

19.

Murphy 4th F, Churchill M . Nonsequence-specific DNA recognition: a structural perspective. Structure. 2000; 8(4):R83-9. DOI: 10.1016/s0969-2126(00)00126-x. View

20.

Kortschak R, Tucker P, Saint R . ARID proteins come in from the desert. Trends Biochem Sci. 2000; 25(6):294-9. DOI: 10.1016/s0968-0004(00)01597-8. View