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Conference Paper: Dissection of biophysical properties and biological activities of Bet/RecT family DNA recombination proteins
Title | Dissection of biophysical properties and biological activities of Bet/RecT family DNA recombination proteins |
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Authors | |
Issue Date | 2014 |
Publisher | The Society for General Microbiology. |
Citation | The 2014 Annual Conference of the Society for General Microbiology, Liverpool, UK., 14-17 April 2014. In Conference Abstracts, 2014, p. 126, abstract no. LI14/08 How to Cite? |
Abstract | Single 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. |
Description | Session LI14: Prokaryotic genetics forum |
Persistent Identifier | http://hdl.handle.net/10722/201145 |
DC Field | Value | Language |
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dc.contributor.author | Chen, W | en_US |
dc.contributor.author | Cheng, T | en_US |
dc.contributor.author | Huang, J | en_US |
dc.contributor.author | Watt, RM | en_US |
dc.date.accessioned | 2014-08-21T07:14:39Z | - |
dc.date.available | 2014-08-21T07:14:39Z | - |
dc.date.issued | 2014 | en_US |
dc.identifier.citation | The 2014 Annual Conference of the Society for General Microbiology, Liverpool, UK., 14-17 April 2014. In Conference Abstracts, 2014, p. 126, abstract no. LI14/08 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/201145 | - |
dc.description | Session LI14: Prokaryotic genetics forum | - |
dc.description.abstract | Single 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.language | eng | en_US |
dc.publisher | The Society for General Microbiology. | - |
dc.relation.ispartof | Annual Conference of the Society for General Microbiology | en_US |
dc.title | Dissection of biophysical properties and biological activities of Bet/RecT family DNA recombination proteins | en_US |
dc.type | Conference_Paper | en_US |
dc.identifier.email | Chen, W: chenwy@hku.hk | en_US |
dc.identifier.email | Cheng, T: chengtfc@hku.hk | en_US |
dc.identifier.email | Huang, J: jdhuang@hku.hk | en_US |
dc.identifier.email | Watt, RM: rmwatt@hku.hk | en_US |
dc.identifier.authority | Chen, W=rp01487 | en_US |
dc.identifier.authority | Huang, J=rp00451 | en_US |
dc.identifier.authority | Watt, RM=rp00043 | en_US |
dc.identifier.hkuros | 233932 | en_US |
dc.identifier.spage | 126, abstract no. LI14/08 | - |
dc.identifier.epage | 126, abstract no. LI14/08 | - |
dc.publisher.place | United Kingdom | - |