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Conference Paper: Dissection of biophysical properties and biological activities of Bet/RecT family DNA recombination proteins

TitleDissection of biophysical properties and biological activities of Bet/RecT family DNA recombination proteins
Authors
Issue Date2014
PublisherThe Society for General Microbiology.
Citation
The Annual Conference of the Society for General Microbiology, Liverpool, United Kingdom, 14 to 17 April 2014. In the Abstracts of the Annual Conference of the Society for General Microbiology, 2014, p. 126, abstract no. LI14/08 How to Cite?
AbstractSingle strand DNA annealing proteins (SSAPs) of viral/phage origin play a variety of roles in homologous recombination-based DNA repair and genetic exchange processes in prokaryotes. Bet from bacteriophage lambda and RecT from Escherichia coli are the prototypical SSAPs. Bet/RecT family SSAP proteins putatively share a conserved multimeric organization and arrangement of secondary structural units. Here, we use a combination of biophysical and biological approaches to dissect structure-activity relationships within a diverse selection of SSAP proteins, including: E. coli RecT; Lambda-Bet; s065 from the SXT genetic element of Vibrio cholerae (SXT-Bet) and Bet from Laribacter hongkongensis (LHK-Bet). Single nucleotide alteration and double strand DNA deletion activities were investigated using E. coli reporter systems. We show that Bet/RecT SSAP proteins that have been rationally-truncated at the N-terminus, but not at the C-terminus, exhibit DNA recombination activities. The removal of specific secondary structural units from Bet/RecT SSAPs profoundly affects protein multimer formation in a complex manner. Binding assays indicate that DNA recombination activities are not directly related to single strand DNA binding abilities. Our results suggest that a complex interplay of protein-protein and protein-nucleotide interactions underlie DNA recombination activities in Bet/RecT family SSAP proteins.
DescriptionSession LI14: Prokaryotic genetics forum
Persistent Identifierhttp://hdl.handle.net/10722/201145

 

DC FieldValueLanguage
dc.contributor.authorChen, Wen_US
dc.contributor.authorCheng, Ten_US
dc.contributor.authorHuang, Jen_US
dc.contributor.authorWatt, RMen_US
dc.date.accessioned2014-08-21T07:14:39Z-
dc.date.available2014-08-21T07:14:39Z-
dc.date.issued2014en_US
dc.identifier.citationThe Annual Conference of the Society for General Microbiology, Liverpool, United Kingdom, 14 to 17 April 2014. In the Abstracts of the Annual Conference of the Society for General Microbiology, 2014, p. 126, abstract no. LI14/08en_US
dc.identifier.urihttp://hdl.handle.net/10722/201145-
dc.descriptionSession LI14: Prokaryotic genetics forum-
dc.description.abstractSingle strand DNA annealing proteins (SSAPs) of viral/phage origin play a variety of roles in homologous recombination-based DNA repair and genetic exchange processes in prokaryotes. Bet from bacteriophage lambda and RecT from Escherichia coli are the prototypical SSAPs. Bet/RecT family SSAP proteins putatively share a conserved multimeric organization and arrangement of secondary structural units. Here, we use a combination of biophysical and biological approaches to dissect structure-activity relationships within a diverse selection of SSAP proteins, including: E. coli RecT; Lambda-Bet; s065 from the SXT genetic element of Vibrio cholerae (SXT-Bet) and Bet from Laribacter hongkongensis (LHK-Bet). Single nucleotide alteration and double strand DNA deletion activities were investigated using E. coli reporter systems. We show that Bet/RecT SSAP proteins that have been rationally-truncated at the N-terminus, but not at the C-terminus, exhibit DNA recombination activities. The removal of specific secondary structural units from Bet/RecT SSAPs profoundly affects protein multimer formation in a complex manner. Binding assays indicate that DNA recombination activities are not directly related to single strand DNA binding abilities. Our results suggest that a complex interplay of protein-protein and protein-nucleotide interactions underlie DNA recombination activities in Bet/RecT family SSAP proteins.en_US
dc.languageengen_US
dc.publisherThe Society for General Microbiology.-
dc.relation.ispartofAnnual Conference of the Society for General Microbiologyen_US
dc.titleDissection of biophysical properties and biological activities of Bet/RecT family DNA recombination proteinsen_US
dc.typeConference_Paperen_US
dc.identifier.emailChen, W: chenwy@hku.hken_US
dc.identifier.emailCheng, T: chengtfc@hku.hken_US
dc.identifier.emailHuang, J: jdhuang@hku.hken_US
dc.identifier.emailWatt, RM: rmwatt@hku.hken_US
dc.identifier.authorityChen, W=rp01487en_US
dc.identifier.authorityHuang, J=rp00451en_US
dc.identifier.authorityWatt, RM=rp00043en_US
dc.identifier.hkuros233932en_US
dc.identifier.spage126, abstract no. LI14/08-
dc.identifier.epage126, abstract no. LI14/08-
dc.publisher.placeUnited Kingdom-

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