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Biochemical and biophysical characte...

Antczak, Andrew James.

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Biochemical and biophysical characterization of the histone chaperone protein Asf1.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Biochemical and biophysical characterization of the histone chaperone protein Asf1./
Author:	Antczak, Andrew James.
Description:	132 p.
Notes:	Adviser: James M. Berger.
Contained By:	Dissertation Abstracts International68-08B.
Subject:	Biology, Bioinformatics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3275331
ISBN:	9780549164975

Biochemical and biophysical characterization of the histone chaperone protein Asf1.
Antczak, Andrew James.

Biochemical and biophysical characterization of the histone chaperone protein Asf1. - 132 p.

Adviser: James M. Berger.

Thesis (Ph.D.)--University of California, Berkeley, 2007.

The histone H3/H4 chaperone Asf1 (anti- silencing function 1) is required for the establishment and maintenance of proper chromatin structure, as well as for genome stability in eukaryotes. Asf1 participates in both DNA synthesis-coupled and synthesis-independent histone deposition reactions in vitro and interacts with complexes responsible for both pathways in vivo, although the reaction mechanisms are poorly understood. Asf1 is known to directly bind histone H3, however, high-resolution structural information about the geometry of this interaction was previously unknown. Additionally, Asf1 interacts with a number of proteins involved in diverse processes within chromatin biology. It is thought that Asf1 functions to couple histone deposition to these different processes.

ISBN: 9780549164975Subjects--Topical Terms:

1018415
Biology, Bioinformatics.

Biochemical and biophysical characterization of the histone chaperone protein Asf1.
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020 $a 9780549164975
035 $a (UMI)AAI3275331
035 $a AAI3275331
040 $a UMI $c UMI
100 1 $a Antczak, Andrew James. $3 1285795
245 1 0 $a Biochemical and biophysical characterization of the histone chaperone protein Asf1.
300 $a 132 p.
500 $a Adviser: James M. Berger.
500 $a Source: Dissertation Abstracts International, Volume: 68-08, Section: B, page: 5199.
502 $a Thesis (Ph.D.)--University of California, Berkeley, 2007.
520 $a The histone H3/H4 chaperone Asf1 (anti- silencing function 1) is required for the establishment and maintenance of proper chromatin structure, as well as for genome stability in eukaryotes. Asf1 participates in both DNA synthesis-coupled and synthesis-independent histone deposition reactions in vitro and interacts with complexes responsible for both pathways in vivo, although the reaction mechanisms are poorly understood. Asf1 is known to directly bind histone H3, however, high-resolution structural information about the geometry of this interaction was previously unknown. Additionally, Asf1 interacts with a number of proteins involved in diverse processes within chromatin biology. It is thought that Asf1 functions to couple histone deposition to these different processes.
520 $a Here we report the identification of several novel Asf1-interacting proteins by mass spectrometry. The identified proteins are involved in nuclear processes including DNA replication, gene transcription, histone and nucleosome modification, and cell cycle regulation. Importantly, we identify a macromolecular complex containing all four yeast Hir proteins and Asf1. We show that Asf1 is able to stimulate DNA synthesis-independent histone deposition by the Hir complex in vitro. Additionally, we identify a number of in vivo phosphorylation sites on Asf1. We show that mutation of several of these residues results in distinct phenotypes both in vitro and in vivo.
520 $a We demonstrate the establishment of a novel and fully recombinant DNA synthesis-coupled histone deposition assay. We use this assay to formally show that Asf1 can deposit histones onto DNA in a synthesis-independent fashion. We also identify a potential reaction intermediate consisting of histones H3/H4 bound to both DNA and the assisting chaperone. Additionally, we demonstrate that Asf1 is able to interact with a histone H3/H4 heterotetramer, an interaction that potentiates histone eviction during DNA replication and gene transcription.
520 $a Finally, we report the structure of a histone/histone chaperone interaction. We have solved the 2.2 A crystal structure of the conserved N-terminal immunoglobulin fold domain of yeast Asf1 (residues 2-155) bound to the C-terminal helix of yeast histone H3 (residues 121-134). The structure defines a histone-binding patch on Asf1 consisting of both conserved and yeast-specific residues; mutation of these residues abrogates H3/H4 binding affinity. The geometry of the interaction indicates that Asf1 binds to histones H3/H4 in a manner that likely blocks sterically the H3/H3 interface of the nucleosomal four-helix bundle. These data clarify how Asf1 regulates histone stoichiometry to modulate epigenetic inheritance. The structure further suggests a physical model in which Asf1 contributes to interpretation of a "histone H3 barcode" for sorting H3 isoforms into different deposition pathways.
590 $a School code: 0028.
650 4 $a Biology, Bioinformatics. $3 1018415
650 4 $a Biology, Molecular. $3 1017719
650 4 $a Chemistry, Biochemistry. $3 1017722
690 $a 0307
690 $a 0487
690 $a 0715
710 2 $a University of California, Berkeley. $3 687832
773 0 $t Dissertation Abstracts International $g 68-08B.
790 $a 0028
790 1 0 $a Berger, James M., $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3275331