Staff View
Evolution of a novel gene pair from a canonical toxin-antitoxin module in Escherichia coli

Descriptive

TypeOfResource
Text
TitleInfo (ID = T-1); (type = uniform)
Title
Evolution of a novel gene pair from a canonical toxin-antitoxin module in Escherichia coli
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10001600001.ETD.17439
Identifier
ETD_1216
Language
LanguageTerm (authority = ISO 639-3:2007)
English
Genre (authority = marcgt)
theses
Subject (ID = SBJ-1); (authority = RUETD)
Topic
Microbiology and Molecular Genetics
Subject (ID = SBJ-2); (authority = ETD-LCSH)
Topic
Toxins
Subject (ID = SBJ-3); (authority = ETD-LCSH)
Topic
Antitoxins
Subject (ID = SBJ-4); (authority = ETD-LCSH)
Topic
Escherichia coli
Abstract
Free-living bacteria are continuously subjected to environmental stress. This stress can be in the form of a change in temperature, pH, osmolarity or nutritional starvation. Most bacterial species contain gene modules known as Toxin-Antitoxin (TA) systems that reversibly inhibit cellular growth in response to stress; thereby helping the cells cope with a changing environment. One mechanism that bacteria have developed to combat fluctuations in environmental temperature is the cold-shock response. This response helps exponentially growing cells buffer themselves against a downshift in temperature from their optimal growing temperature; typically a shift from 37??C to 15??C for Escherichia coli (E. coli). Cold-shock proteins (Csp) are synthesized at this time. Protein Y (PY), the protein product of gene yfiA in E. coli is suggested to be a cold-shock related protein. It prevents ribosomes from dissociation during cold-shock, and in stationary phase, thereby blocking translational elongation and inhibiting cell growth. This mechanism resembled that of a typical TA system toxin. We identified a small gene, b2596, upstream of yfiA and propose that the b2596-yfiA module evolved from a true proteic TA system that functioned in cold-shock conditions; Protein X (PX), product of b2596, being the antitoxin and PY the toxin. The module still retains some of its TA system characteristics: both genes encode small proteins, have opposing charges and show sequence similarity to known TA genes. Also, like a true TA system b2596, the proposed antitoxin gene, precedes yfiA, the proposed toxin gene. However, we found that the two genes have independent transcriptional start sites. Also b2596 encodes a leaderless mRNA with UUG start and thus we predict that it cannot be translated well in vivo. PY inhibits growth of E. coli cells and functions in helping the bacterial population to survive cold-shock. Our data suggest that b2596 and yfiA have evolved from a canonical proteic TA module that was functional in cold shock. The two genes are now independent and responsive to cold shock.
PhysicalDescription
Extent
vii, 60 pages
InternetMediaType
application/pdf
InternetMediaType
text/xml
Note (type = degree)
M.S.
Note (type = bibliography)
Includes bibliographical references (p. 56-60).
Name (ID = NAME-1); (type = personal)
NamePart (type = family)
Bhanot
NamePart (type = given)
Tamanna Devraj
Role
RoleTerm (authority = RUETD)
author
DisplayForm
Tamanna Devraj Bhanot
Name (ID = NAME-2); (type = personal)
NamePart (type = family)
Woychik
NamePart (type = given)
Nancy
Role
RoleTerm (authority = RULIB)
chair
Affiliation
Advisory Committee
DisplayForm
Nancy Ann Woychik
Name (ID = NAME-3); (type = personal)
NamePart (type = family)
Vershon
NamePart (type = given)
Andrew
Role
RoleTerm (authority = RULIB)
internal member
Affiliation
Advisory Committee
DisplayForm
Andrew K Vershon
Name (ID = NAME-4); (type = personal)
NamePart (type = family)
Phadatre
NamePart (type = given)
Sangita
Role
RoleTerm (authority = RULIB)
internal member
Affiliation
Advisory Committee
DisplayForm
Sangita Phadatre
Name (ID = NAME-1); (type = corporate)
NamePart
Rutgers University
Role
RoleTerm (authority = RULIB)
degree grantor
Name (ID = NAME-2); (type = corporate)
NamePart
Graduate School - New Brunswick
Role
RoleTerm (authority = RULIB)
school
OriginInfo
DateCreated (qualifier = exact)
2008
DateOther (qualifier = exact); (type = degree)
2008-10
Location
PhysicalLocation (authority = marcorg)
NjNbRU
RelatedItem (type = host)
TitleInfo
Title
Graduate School - New Brunswick Electronic Theses and Dissertations
Identifier (type = local)
rucore19991600001
Identifier (type = doi)
doi:10.7282/T3Q81DFJ
Genre (authority = ExL-Esploro)
ETD graduate
Back to the top

Rights

RightsDeclaration (AUTHORITY = GS); (ID = rulibRdec0006)
The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
AssociatedEntity (AUTHORITY = rulib); (ID = 1)
Name
Tamanna Bhanot
Role
Copyright holder
Affiliation
Rutgers University. Graduate School - New Brunswick
RightsEvent (AUTHORITY = rulib); (ID = 1)
Type
Permission or license
Detail
Non-exclusive ETD license
AssociatedObject (AUTHORITY = rulib); (ID = 1)
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.
Back to the top

Technical

Format (TYPE = mime); (VERSION = )
application/x-tar
FileSize (UNIT = bytes)
2204160
Checksum (METHOD = SHA1)
31ad68fdb858d0e282662e010c78249c55b0fc31
ContentModel
ETD
CompressionScheme
other
OperatingSystem (VERSION = 5.1)
windows xp
Format (TYPE = mime); (VERSION = NULL)
application/x-tar
Back to the top
Version 8.3.13
Rutgers University Libraries - Copyright ©2021