NDLI: Human STAGA Complex Is a Chromatin-Acetylating Transcription Coactivator That Interacts with Pre-mRNA Splicing and DNA Damage-Binding Factors In Vivo

Content Provider	PubMed Central
Author	Martinez, Ernest Palhan, Vikas B. Tjernberg, Agneta Lymar, Elena S. Gamper, Armin M. Kundu, Tapas K. Chait, Brian T. Roeder, Robert G.
Copyright Year	2001
Abstract	GCN5 is a histone acetyltransferase (HAT) originally identified in Saccharomyces cerevisiae and required for transcription of specific genes within chromatin as part of the SAGA (SPT-ADA-GCN5 acetylase) coactivator complex. Mammalian cells have two distinct GCN5 homologs (PCAF and GCN5L) that have been found in three different SAGA-like complexes (PCAF complex, TFTC [TATA-binding-protein-free TAFII-containing complex], and STAGA [SPT3-TAFII31-GCN5L acetylase]). The composition and roles of these mammalian HAT complexes are still poorly characterized. Here, we present the purification and characterization of the human STAGA complex. We show that STAGA contains homologs of most yeast SAGA components, including two novel human proteins with histone-like folds and sequence relationships to yeast SPT7 and ADA1. Furthermore, we demonstrate that STAGA has acetyl coenzyme A-dependent transcriptional coactivator functions from a chromatin-assembled template in vitro and associates in HeLa cells with spliceosome-associated protein 130 (SAP130) and DDB1, two structurally related proteins. SAP130 is a component of the splicing factor SF3b that associates with U2 snRNP and is recruited to prespliceosomal complexes. DDB1 (p127) is a UV-damaged-DNA-binding protein that is involved, as part of a complex with DDB2 (p48), in nucleotide excision repair and the hereditary disease xeroderma pigmentosum. Our results thus suggest cellular roles of STAGA in chromatin modification, transcription, and transcription-coupled processes through direct physical interactions with sequence-specific transcription activators and with components of the splicing and DNA repair machineries.
Related Links	http://dx.doi.org/10.1128/mcb.21.20.6782-6795.2001
Ending Page	6795
Page Count	14
Starting Page	6782
File Format	PDF
ISSN	02707306
e-ISSN	10985549
Journal	Molecular and Cellular Biology
Issue Number	20
Volume Number	21
Language	English
Publisher	American Society for Microbiology
Publisher Date	2001-10-15
Access Restriction	Open
Rights Holder	American Society for Microbiology
Subject Keyword	Cell Biology Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The RNA Splicing Response to DNA Damage

Multivalent Binding of p53 to the STAGA Complex Mediates Coactivator Recruitment after UV Damage▿

MYC interacts with the human STAGA coactivator complex via multivalent contacts with the GCN5 and TRRAP subunits

MYC interacts with the human STAGA coactivator complex via multivalent contacts with the GCN5 and TRRAP subunits.

Exo70, a subunit of the exocyst complex, interacts with SNEVhPrp19/hPso4 and is involved in pre-mRNA splicing

Human ATAC Is a GCN5/PCAF-containing Acetylase Complex with a Novel NC2-like Histone Fold Module That Interacts with the TATA-binding Protein

Human Splicing Factor SF3a, but Not SF1, Is Essential for Pre-mRNA Splicing In Vivo

MYC interacts with the human STAGA coactivator complex via multivalent contacts with the GCN5 and TRRAP subunits

RAP250 Is a Coactivator in the Transforming Growth Factor β Signaling Pathway That Interacts with Smad2 and Smad3

Human STAGA Complex Is a Chromatin-Acetylating Transcription Coactivator That Interacts with Pre-mRNA Splicing and DNA Damage-Binding Factors In Vivo

Similar Documents

The RNA Splicing Response to DNA Damage

Multivalent Binding of p53 to the STAGA Complex Mediates Coactivator Recruitment after UV Damage▿

MYC interacts with the human STAGA coactivator complex via multivalent contacts with the GCN5 and TRRAP subunits

MYC interacts with the human STAGA coactivator complex via multivalent contacts with the GCN5 and TRRAP subunits.

Exo70, a subunit of the exocyst complex, interacts with SNEVhPrp19/hPso4 and is involved in pre-mRNA splicing

Human ATAC Is a GCN5/PCAF-containing Acetylase Complex with a Novel NC2-like Histone Fold Module That Interacts with the TATA-binding Protein

Human Splicing Factor SF3a, but Not SF1, Is Essential for Pre-mRNA Splicing In Vivo

MYC interacts with the human STAGA coactivator complex via multivalent contacts with the GCN5 and TRRAP subunits

RAP250 Is a Coactivator in the Transforming Growth Factor β Signaling Pathway That Interacts with Smad2 and Smad3

Human STAGA Complex Is a Chromatin-Acetylating Transcription Coactivator That Interacts with Pre-mRNA Splicing and DNA Damage-Binding Factors In Vivo