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Mass spectrometric analysis of post-...

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Mass spectrometric analysis of post-translational modifications of histone and histone-like proteins.

Record Type:	Language materials, printed : Monograph/item
Title/Author:	Mass spectrometric analysis of post-translational modifications of histone and histone-like proteins./
Author:	Muratore, Tara Lynn.
Description:	162 p.
Notes:	Adviser: Donald F. Hunt.
Contained By:	Dissertation Abstracts International67-10B.
Subject:	Chemistry, Analytical. -
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3238136
ISBN:	9780542923609

Mass spectrometric analysis of post-translational modifications of histone and histone-like proteins.
Muratore, Tara Lynn.

Mass spectrometric analysis of post-translational modifications of histone and histone-like proteins. - 162 p.

Adviser: Donald F. Hunt.

Thesis (Ph.D.)--University of Virginia, 2007.

Post-translational modifications (PTMs) play a critical role in many biological processes, such as gene expression, cell signaling and mitosis. Alterations to these processes are known to be characteristic of cellular disease states, most notably cancer. It is crucial to characterize the PTMs of proteins that mediate these cellular processes. Mass spectrometry is a powerful tool for studying PTMs. Presented herein are three examples of the imperative use of mass spectrometry to characterize the PTMs of histone and histone-like proteins to help solve biological problems. The high resolution mass spectrometer, LTQ-FTMS, offers accurate mass measurement. Tandem mass spectrometry using collision activated dissociation or electron transfer dissociation, a newly developed fragmentation technique, make it possible to sequence peptides and unambiguously assign the specific sites of modification.

ISBN: 9780542923609Subjects--Topical Terms:

586156
Chemistry, Analytical.

Mass spectrometric analysis of post-translational modifications of histone and histone-like proteins.
LDR:03407nam 2200301 a 45 001 969379
005 20110920
008 110921s2007 eng d
020 $a 9780542923609
035 $a (UMI)AAI3238136
035 $a AAI3238136
040 $a UMI $c UMI
100 1 $a Muratore, Tara Lynn. $3 1293432
245 1 0 $a Mass spectrometric analysis of post-translational modifications of histone and histone-like proteins.
300 $a 162 p.
500 $a Adviser: Donald F. Hunt.
500 $a Source: Dissertation Abstracts International, Volume: 67-10, Section: B, page: 5717.
502 $a Thesis (Ph.D.)--University of Virginia, 2007.
520 $a Post-translational modifications (PTMs) play a critical role in many biological processes, such as gene expression, cell signaling and mitosis. Alterations to these processes are known to be characteristic of cellular disease states, most notably cancer. It is crucial to characterize the PTMs of proteins that mediate these cellular processes. Mass spectrometry is a powerful tool for studying PTMs. Presented herein are three examples of the imperative use of mass spectrometry to characterize the PTMs of histone and histone-like proteins to help solve biological problems. The high resolution mass spectrometer, LTQ-FTMS, offers accurate mass measurement. Tandem mass spectrometry using collision activated dissociation or electron transfer dissociation, a newly developed fragmentation technique, make it possible to sequence peptides and unambiguously assign the specific sites of modification.
520 $a The first study focused on the investigation of heterochromatin; the regions of chromatin that contain transcriptionally silenced genes. Methylation of histone H3, catalyzed by methyltransferases, and recruitment of chromodomain-containing proteins are linked to heterochromatin formation. To identify the lysine substrates of specific methyltransferases, modification patterns of H3 isolated from WT Tetrahymena were compared to the modification patterns of H3 isolated from a mutated Tetrahymena strain, in which a gene that encodes for a specific methyltransferase was knocked out.
520 $a In the second study, a global analysis was performed on the histone-like protein, RCC1. The N-terminal region of RCC1 is highly basic and similar to that of the N-terminal tail of H3. RCC1 is responsible for catalyzing the formation of RanGTP, which is essential for mitotic spindle assembly and nuclear envelope formation. Rare PTMs of RCC1 were identified and various biochemical experiments showed that inhibition of these modifications caused mitotic defects.
520 $a Lastly, we were interested in understanding the mechanisms involved in embryonic stem (ES) cell differentiation, the process that defines specialized cells. During the differentiation process, many genes are destined to be turned "on" or "off'. Histone PTMs and their associated proteins are implicated in ES cell differentiation. We identified a proteolyically cleaved H3 protein associated with cell differentiation. MS analyses identified the specific sites of cleavage and characterized the PTMs on the cleaved H3 protein.
590 $a School code: 0246.
650 4 $a Chemistry, Analytical. $3 586156
690 $a 0486
710 2 0 $a University of Virginia. $3 645578
773 0 $t Dissertation Abstracts International $g 67-10B.
790 $a 0246
790 1 0 $a Hunt, Donald F., $e advisor
791 $a Ph.D.
792 $a 2007
856 4 0 $u http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3238136