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Functions of the MYST family histone...

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Functions of the MYST family histone acetyltransferase Esa1 of Saccharomyces cerevisiae.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Functions of the MYST family histone acetyltransferase Esa1 of Saccharomyces cerevisiae./
Author:	Decker, Peter Vincent.
Description:	163 p.
Notes:	Adviser: M. Mitchell Smith.
Contained By:	Dissertation Abstracts International68-09B.
Subject:	Biology, Genetics. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3282482
ISBN:	9780549247838

Functions of the MYST family histone acetyltransferase Esa1 of Saccharomyces cerevisiae.
Decker, Peter Vincent.

Functions of the MYST family histone acetyltransferase Esa1 of Saccharomyces cerevisiae. - 163 p.

Adviser: M. Mitchell Smith.

Thesis (Ph.D.)--University of Virginia, 2008.

Eas1 is the only histone acetyltransferase in Saccharomyces cerevisiae that is essential for viability. This enzymatic activity, directed primarily towards histone H4, has lone been thought to be the essential function of Eas1 and its constituent NuA4 and Piccolo NuA4 complexes. However, no study to date has formally shown that catalysis is indispensable. Here we present evidence that the essential function of Eas1 does not involve its histone acetylation function. We show that a catalytically dead eas1 allele supports viability, and that loss of histone H4 acetylation by Eas1 correlates with sensitivity to a variety of stress agents. Strikingly, while catalysis is not required for viability, a structurally intact catalytic pocket does appear vital, suggesting that the essential function of Eas1 may involve cofactor and/or substrate recognition. To further understand the nature of the essential function of Eas1, we have also carried out a second-site suppressor screen with a thermolabile esa1 allele. Two hits from the screen are components of the Rpd3L histone deacetylase complex, which has many functions that oppose those of NuA4 and Eas1. Surprisingly, the balance of histone acetylation and deacetylation may not play a prominent role in suppression. We propose a model in which Eas1 is an essential regulatory subunit of NuA4 activities, which include but are not limited to histone acetylation, and that loss of Eas1 results in catastrophic misregulation of one or more essential processes, leading to cell death.

ISBN: 9780549247838Subjects--Topical Terms:

1017730
Biology, Genetics.

Functions of the MYST family histone acetyltransferase Esa1 of Saccharomyces cerevisiae.
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020 $a 9780549247838
035 $a (UMI)AAI3282482
035 $a AAI3282482
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100 1 $a Decker, Peter Vincent. $3 1017729
245 1 0 $a Functions of the MYST family histone acetyltransferase Esa1 of Saccharomyces cerevisiae.
300 $a 163 p.
500 $a Adviser: M. Mitchell Smith.
500 $a Source: Dissertation Abstracts International, Volume: 68-09, Section: B, page: 5711.
502 $a Thesis (Ph.D.)--University of Virginia, 2008.
520 $a Eas1 is the only histone acetyltransferase in Saccharomyces cerevisiae that is essential for viability. This enzymatic activity, directed primarily towards histone H4, has lone been thought to be the essential function of Eas1 and its constituent NuA4 and Piccolo NuA4 complexes. However, no study to date has formally shown that catalysis is indispensable. Here we present evidence that the essential function of Eas1 does not involve its histone acetylation function. We show that a catalytically dead eas1 allele supports viability, and that loss of histone H4 acetylation by Eas1 correlates with sensitivity to a variety of stress agents. Strikingly, while catalysis is not required for viability, a structurally intact catalytic pocket does appear vital, suggesting that the essential function of Eas1 may involve cofactor and/or substrate recognition. To further understand the nature of the essential function of Eas1, we have also carried out a second-site suppressor screen with a thermolabile esa1 allele. Two hits from the screen are components of the Rpd3L histone deacetylase complex, which has many functions that oppose those of NuA4 and Eas1. Surprisingly, the balance of histone acetylation and deacetylation may not play a prominent role in suppression. We propose a model in which Eas1 is an essential regulatory subunit of NuA4 activities, which include but are not limited to histone acetylation, and that loss of Eas1 results in catastrophic misregulation of one or more essential processes, leading to cell death.
590 $a School code: 0246.
650 4 $a Biology, Genetics. $3 1017730
650 4 $a Biology, Molecular. $3 1017719
690 $a 0307
690 $a 0369
710 2 $a University of Virginia. $3 645578
773 0 $t Dissertation Abstracts International $g 68-09B.
790 $a 0246
790 1 0 $a Smith, M. Mitchell, $e advisor
791 $a Ph.D.
792 $a 2008
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3282482