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A lysine desert protects sumo-targeted Ub ligases from auto-ubiquitination and proteolysis to maintain genome stability in yeast
Descriptive
TitleInfo
Title
A lysine desert protects sumo-targeted Ub ligases from auto-ubiquitination and proteolysis to maintain genome stability in yeast
Name
(type = personal)
NamePart
(type = family)
Sharma
NamePart
(type = given)
Pragati
NamePart
(type = date)
1984-
DisplayForm
Pragati Sharma
Role
RoleTerm
(authority = RULIB)
author
Name
(type = personal)
NamePart
(type = family)
Brill
NamePart
(type = given)
Steven J
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Steven J Brill
Affiliation
Advisory Committee
Role
RoleTerm
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chair
Name
(type = personal)
NamePart
(type = family)
Madura
NamePart
(type = given)
Kiran
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Kiran Madura
Affiliation
Advisory Committee
Role
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(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Zaratiegui
NamePart
(type = given)
Mikel
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Mikel Zaratiegui
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Advisory Committee
Role
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(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Gartenberg
NamePart
(type = given)
Marc R
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Marc R Gartenberg
Affiliation
Advisory Committee
Role
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(authority = RULIB)
outside member
Name
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NamePart
Rutgers University
Role
RoleTerm
(authority = RULIB)
degree grantor
Name
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NamePart
Graduate School - New Brunswick
Role
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school
TypeOfResource
Text
Genre
(authority = marcgt)
theses
OriginInfo
DateCreated
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2015
DateOther
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(type = degree)
2015-01
CopyrightDate
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(qualifier = exact)
2015
Place
PlaceTerm
(type = code)
xx
Language
LanguageTerm
(authority = ISO639-2b);
(type = code)
eng
Abstract
(type = abstract)
Post-translational modification by SUMO (Small Ubiquitin-like MOdifier) regulates the enzymatic activity, subcellular localization, and protein-protein interactions of modified target proteins. SUMO has also been implicated in proteasome-dependent protein degradation with the identification of a special class of enzymes termed, SUMO-Targeted Ubiquitin Ligases (STUbLs). These conserved enzymes typically possess multiple, tandem SUMO-Interaction Motifs and a RING domain that together facilitate the conjugation of ubiquitin to SUMO-modified target proteins. Originally discovered as essential gene pair for the viability of RecQ helicase-deficient yeast, SLX5 and SLX8 code for a heterodimeric STUbL. Two novel alleles of SLX5 were isolated in a forward genetic screen for suppressors of genome instability. A combination of genetic and biochemical experiments indicate that these alleles disrupt a conserved lysine desert, unique to STUbLs, leading to Slx5’s auto-ubiquitination and proteasome-mediated degradation. The results are consistent with the idea that STUbLs employ a lysine desert as a defense against self-destruction.
Subject
(authority = RUETD)
Topic
Biochemistry
Subject
(authority = ETD-LCSH)
Topic
Lysine
Subject
(authority = ETD-LCSH)
Topic
Ubiquitin
Subject
(authority = ETD-LCSH)
Topic
Yeast
RelatedItem
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TitleInfo
Title
Rutgers University Electronic Theses and Dissertations
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ETD
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ETD_6150
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electronic resource
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application/pdf
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text/xml
Extent
1 online resource (ix, 128 p. : ill.)
Note
(type = degree)
Ph.D.
Note
(type = bibliography)
Includes bibliographical references
Note
(type = statement of responsibility)
by Pragati Sharma
RelatedItem
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TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier
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rucore19991600001
Location
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(displayLabel = Rutgers, The State University of New Jersey)
NjNbRU
Identifier
(type = doi)
doi:10.7282/T36H4K31
Genre
(authority = ExL-Esploro)
ETD doctoral
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Rights
RightsDeclaration
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The author owns the copyright to this work.
RightsHolder
(type = personal)
Name
FamilyName
Sharma
GivenName
Pragati
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime
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(qualifier = exact);
(point = start)
2015-01-05 12:09:44
AssociatedEntity
Name
Pragati Sharma
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
AssociatedObject
Type
License
Name
Author Agreement License
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
RightsEvent
DateTime
(encoding = w3cdtf);
(qualifier = exact);
(point = start)
2015-01-31
DateTime
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(qualifier = exact);
(point = end)
2016-01-31
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after January 31st, 2016.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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Technical
RULTechMD
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ContentModel
ETD
OperatingSystem
(VERSION = 5.1)
windows xp
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