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Identification and characterization of Mycobacterium tuberculosis VapC50 toxin
Descriptive
TitleInfo
Title
Identification and characterization of Mycobacterium tuberculosis VapC50 toxin
Name
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NamePart
(type = family)
Cortese
NamePart
(type = given)
Jillian Nicole
NamePart
(type = date)
1992-
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Jillian Nicole Cortese
Role
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(authority = RULIB)
author
Name
(type = personal)
NamePart
(type = family)
Boyd
NamePart
(type = given)
Jeff
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Jeff Boyd
Affiliation
Advisory Committee
Role
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(authority = RULIB)
chair
Name
(type = personal)
NamePart
(type = family)
Woychik
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Nancy
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Nancy Woychik
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Advisory Committee
Role
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(authority = RULIB)
internal member
Name
(type = personal)
NamePart
(type = family)
Fan
NamePart
(type = given)
Huizhou
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Huizhou Fan
Affiliation
Advisory Committee
Role
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(authority = RULIB)
internal 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
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school
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Text
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theses
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2017
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2017-01
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2017
Place
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xx
Language
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eng
Abstract
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Tuberculosis is a major health concern for a large portion of the world’s population, despite its reputation as an ancient disease. One of the main concerns is the development of latent tuberculosis, where Mycobacterium tuberculosis remains dormant for months or years before being reactivated. Among all bacteria studied thus far, M. tuberculosis has the most toxin-antitoxin (TA) systems, with 88 discovered so far, 50 of which are VapBC systems. It is thought that these TA systems may aid the bacteria in establishing and/or maintaining M. tuberculosis cells in this nonreplicating persistent state characteristic of latent tuberculosis. TA systems have been shown to respond to various stressors that bacteria may encounter, including hypoxia, host immune responses, and nutrient starvation. VapBC, which is a type II TA system, is composed of an unstable antitoxin protein, VapB, that binds to the stable PIN domain-containing VapC toxin protein and blocks its activity. The goals of this M.S. research project were to isolate, characterize and identify the RNA target of one M. tuberculosis VapC toxin, VapC50. To this end, we first discovered that the annotated VapC50 gene was incorrect, and instead identified and cloned the correct VapC50 toxin. Expression of VapC50 in Escherichia coli resulted in growth inhibition, however, expression Mycobacterium smegmatis did not inhibit growth. Purification of recombinant VapC50 protein proved to be a difficult task and was only successful after the third trial, when the protein was expressed at 30C instead of 37C. Since most of the analysis of VapC toxins published highlight their tRNA cleaving ability, purified VapC50 was used to conduct a tRNA cleavage assay with all 45 tRNAs in M. tuberculosis. None of the 45 tRNAs were cleaved by VapC50, suggesting that this toxin may instead have a novel physiological role in this pathogen.
Subject
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Topic
Microbiology and Molecular Genetics
Subject
(authority = ETD-LCSH)
Topic
Mycobacterium tuberculosis
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Title
Rutgers University Electronic Theses and Dissertations
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ETD_7870
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electronic resource
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application/pdf
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text/xml
Extent
1 online resource (ix, 70 p. : ill.)
Note
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M.S.
Note
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Includes bibliographical references
Note
(type = statement of responsibility)
by Jillian Nicole Cortese
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TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
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rucore19991600001
Location
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NjNbRU
Identifier
(type = doi)
doi:10.7282/T3CJ8GXZ
Genre
(authority = ExL-Esploro)
ETD graduate
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Rights
RightsDeclaration
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The author owns the copyright to this work.
RightsHolder
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Name
FamilyName
Cortese
GivenName
Jillian
MiddleName
Nicole
Role
Copyright Holder
RightsEvent
Type
Permission or license
DateTime
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2017-01-13 12:54:28
AssociatedEntity
Name
Jillian Cortese
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
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2017-01-31
DateTime
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2018-01-31
Type
Embargo
Detail
Access to this PDF has been restricted at the author's request. It will be publicly available after January 31st, 2018.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
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Technical
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ETD
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windows xp
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2017-01-13T20:56:37
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2017-01-13T20:56:37
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