Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit. Export

@article{citeulike:1954274, abstract = {Promoter-specific recruitment of histone acetyltransferase activity is often critical for transcriptional activation. We present a detailed study of the interaction between the histone acetyltransferase complexes SAGA and NuA4, and transcription activators. We demonstrate by affinity chromatography and photo-cross-linking label transfer that acidic activators directly interact with Tra1p, a shared subunit of SAGA and NuA4. Mutations within the COOH-terminus of Tra1p disrupted its interaction with activators and resulted in gene-specific transcriptional defects that correlated with lowered promoter-specific histone acetylation. These data demonstrate that the essential Tra1 protein serves as a common target for activators in both SAGA and NuA4 acetyltransferases.}, address = {Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, Department of Chemistry, The Pennsylvania State University, 306 Althouse Laboratory, University Park, PA 16802, USA.}, author = {Brown, C. E. and Howe, L. and Sousa, K. and Alley, S. C. and Carrozza, M. J. and Tan, S. and Workman, J. L.}, citeulike-article-id = {1954274}, citeulike-linkout-0 = {http://dx.doi.org/10.1126/science.1060214}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/11423663}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=11423663}, day = {22}, doi = {10.1126/science.1060214}, issn = {0036-8075}, journal = {Science}, keywords = {crosslinking, in-vitro, tra1}, month = {June}, number = {5525}, pages = {2333--2337}, posted-at = {2008-07-19 19:23:11}, priority = {2}, title = {Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit.}, url = {http://dx.doi.org/10.1126/science.1060214}, volume = {292}, year = {2001} }

TY - JOUR ID - citeulike:1954274 L3 - citeulike-article-id:1954274 N2 - Promoter-specific recruitment of histone acetyltransferase activity is often critical for transcriptional activation. We present a detailed study of the interaction between the histone acetyltransferase complexes SAGA and NuA4, and transcription activators. We demonstrate by affinity chromatography and photo-cross-linking label transfer that acidic activators directly interact with Tra1p, a shared subunit of SAGA and NuA4. Mutations within the COOH-terminus of Tra1p disrupted its interaction with activators and resulted in gene-specific transcriptional defects that correlated with lowered promoter-specific histone acetylation. These data demonstrate that the essential Tra1 protein serves as a common target for activators in both SAGA and NuA4 acetyltransferases. IS - 5525 JF - Science SN - 0036-8075 AD - Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, Department of Chemistry, The Pennsylvania State University, 306 Althouse Laboratory, University Park, PA 16802, USA. EP - 2337 TI - Recruitment of HAT complexes by direct activator interactions with the ATM-related Tra1 subunit. VL - 292 SP - 2333 KW - crosslinking KW - in-vitro KW - tra1 AU - Brown, CE AU - Howe, L AU - Sousa, K AU - Alley, SC AU - Carrozza, MJ AU - Tan, S AU - Workman, JL PY - 2001/06/22/ UR - http://dx.doi.org/10.1126/science.1060214 ER -