The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinity.

Bacteriophage Φ11 uses Staphylococcus aureus as its host and, like lambdoid phages, harbors three homologous operators in between its two divergently oriented repressor genes. None of the repressors of Φ11, however, showed binding to all three operators, even at high concentrations. To understand wh...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Anindya Biswas, Sukhendu Mandal, Subrata Sau
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/22c16663e6a743deaf58f0157cd6730c
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:22c16663e6a743deaf58f0157cd6730c
record_format	dspace
spelling	oai:doaj.org-article:22c16663e6a743deaf58f0157cd6730c2021-11-18T08:22:30ZThe N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinity.1932-620310.1371/journal.pone.0095012https://doaj.org/article/22c16663e6a743deaf58f0157cd6730c2014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24747758/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Bacteriophage Φ11 uses Staphylococcus aureus as its host and, like lambdoid phages, harbors three homologous operators in between its two divergently oriented repressor genes. None of the repressors of Φ11, however, showed binding to all three operators, even at high concentrations. To understand why the DNA binding mechanism of Φ11 repressors does not match that of lambdoid phage repressors, we studied the N-terminal domain of the Φ11 lysogenic repressor, as it harbors a putative helix-turn-helix motif. Our data revealed that the secondary and tertiary structures of the N-terminal domain were different from those of the full-length repressor. Nonetheless, the N-terminal domain was able to dimerize and bind to the operators similar to the intact repressor. In addition, the operator base specificity, binding stoichiometry, and binding mechanism of this domain were nearly identical to those of the whole repressor. The binding affinities of the repressor and its N-terminal domain were reduced to a similar extent when the temperature was increased to 42°C. Both proteins also adequately dislodged a RNA polymerase from a Φ11 DNA fragment carrying two operators and a promoter. Unlike the intact repressor, the binding of the N-terminal domain to two adjacent operator sites was not cooperative in nature. Taken together, we suggest that the dimerization and DNA binding abilities of the N-terminal domain of the Φ11 repressor are distinct from those of the DNA binding domains of other phage repressors.Anindya BiswasSukhendu MandalSubrata SauPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 4, p e95012 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Anindya Biswas Sukhendu Mandal Subrata Sau The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinity.
description	Bacteriophage Φ11 uses Staphylococcus aureus as its host and, like lambdoid phages, harbors three homologous operators in between its two divergently oriented repressor genes. None of the repressors of Φ11, however, showed binding to all three operators, even at high concentrations. To understand why the DNA binding mechanism of Φ11 repressors does not match that of lambdoid phage repressors, we studied the N-terminal domain of the Φ11 lysogenic repressor, as it harbors a putative helix-turn-helix motif. Our data revealed that the secondary and tertiary structures of the N-terminal domain were different from those of the full-length repressor. Nonetheless, the N-terminal domain was able to dimerize and bind to the operators similar to the intact repressor. In addition, the operator base specificity, binding stoichiometry, and binding mechanism of this domain were nearly identical to those of the whole repressor. The binding affinities of the repressor and its N-terminal domain were reduced to a similar extent when the temperature was increased to 42°C. Both proteins also adequately dislodged a RNA polymerase from a Φ11 DNA fragment carrying two operators and a promoter. Unlike the intact repressor, the binding of the N-terminal domain to two adjacent operator sites was not cooperative in nature. Taken together, we suggest that the dimerization and DNA binding abilities of the N-terminal domain of the Φ11 repressor are distinct from those of the DNA binding domains of other phage repressors.
format	article
author	Anindya Biswas Sukhendu Mandal Subrata Sau
author_facet	Anindya Biswas Sukhendu Mandal Subrata Sau
author_sort	Anindya Biswas
title	The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinity.
title_short	The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinity.
title_full	The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinity.
title_fullStr	The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinity.
title_full_unstemmed	The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinity.
title_sort	n-terminal domain of the repressor of staphylococcus aureus phage φ11 possesses an unusual dimerization ability and dna binding affinity.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/22c16663e6a743deaf58f0157cd6730c
work_keys_str_mv	AT anindyabiswas thenterminaldomainoftherepressorofstaphylococcusaureusphageph11possessesanunusualdimerizationabilityanddnabindingaffinity AT sukhendumandal thenterminaldomainoftherepressorofstaphylococcusaureusphageph11possessesanunusualdimerizationabilityanddnabindingaffinity AT subratasau thenterminaldomainoftherepressorofstaphylococcusaureusphageph11possessesanunusualdimerizationabilityanddnabindingaffinity AT anindyabiswas nterminaldomainoftherepressorofstaphylococcusaureusphageph11possessesanunusualdimerizationabilityanddnabindingaffinity AT sukhendumandal nterminaldomainoftherepressorofstaphylococcusaureusphageph11possessesanunusualdimerizationabilityanddnabindingaffinity AT subratasau nterminaldomainoftherepressorofstaphylococcusaureusphageph11possessesanunusualdimerizationabilityanddnabindingaffinity
_version_	1718421848437293056

The N-terminal domain of the repressor of Staphylococcus aureus phage Φ11 possesses an unusual dimerization ability and DNA binding affinity.

Ejemplares similares