This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. Eukaryotic DNA is packed in nucleosomal particles for assembly into high-order structures in the nucleus. Histone modifications in patterns mediated by numerous protein complexes are important for almost all DNA-related processes. Chromatin remodelling complexes can be grouped into two categories depending on nucleosomal conformational alteration or chromatin conformational alteration.Histone acetylation is responsible for chromatin conformational alteration, while Histone acetyltransferases (HATs) are the catalytic subunits of large multiprotein complexes that acetylate the N-terminal tail regions of histones to facilitate transcription activation in eukaryotes.Structural bases for histone modifications mediated by protein-protein complexes are critical to understand these processes. Although during past one decade, significant structural progresses are obtained to understand histone posttranslational modifications including acetylation, phosphorylation, methylation and ubiquitination [reviewed in 4], there are still a lot of unanswered questions: such as how many hotspots exist for modification within histone tails, how many different structural modules can recognize one single histone modification, how many different histone modification sites a single structural module can recognize, how many structural modules can be combined to recognize one single histone modification. In the long term, I would like to answer all these fundamental questions from the structural and molecular view by targeting several critical histone supercomplexes. At this proposal, I outline below a combination of structural and biochemical approaches to study protein-peptide recognition and protein-protein interaction events associated with Histone Code, such as Rtt109 complex mediated H3K56 acetylation and NuA4 complex mediated H4K16 acetylation

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
5P41RR012408-15
Application #
8363357
Study Section
Special Emphasis Panel (ZRG1-BCMB-R (40))
Project Start
2011-07-01
Project End
2012-06-30
Budget Start
2011-07-01
Budget End
2012-06-30
Support Year
15
Fiscal Year
2011
Total Cost
$7,848
Indirect Cost
Name
Brookhaven National Laboratory
Department
Type
DUNS #
027579460
City
Upton
State
NY
Country
United States
Zip Code
11973
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