2jeu: Difference between revisions

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==Overview==

Redox changes are one of the factors that influence cell-cycle progression, and that control the processes of cellular proliferation, differentiation, senescence and apoptosis. Proteins regulated through redox-sensitive, cysteines have been characterized but specific 'sulphydryl switches' in, replication proteins remain to be identified. In bovine papillomavirus, type-1, DNA replication begins when the viral transcription factor E2, recruits the viral initiator protein E1 to the origin of DNA replication, (ori). Here we show that a novel dimerization interface in the E2, transcription activation domain is stabilized by a disulphide bond., Oxidative cross-linking via Cys57 sequesters the interaction surface, between E1 and E2, preventing pre-initiation and replication initiation, complex formation. Our data demonstrate that as well as a mechanism for, regulating DNA binding, redox reactions can control replication by, modulating the tertiary structure of critical protein factors using a, specific redox sensor.

Redox changes are one of the factors that influence cell-cycle progression and that control the processes of cellular proliferation, differentiation, senescence and apoptosis. Proteins regulated through redox-sensitive cysteines have been characterized but specific 'sulphydryl switches' in replication proteins remain to be identified. In bovine papillomavirus type-1, DNA replication begins when the viral transcription factor E2 recruits the viral initiator protein E1 to the origin of DNA replication (ori). Here we show that a novel dimerization interface in the E2 transcription activation domain is stabilized by a disulphide bond. Oxidative cross-linking via Cys57 sequesters the interaction surface between E1 and E2, preventing pre-initiation and replication initiation complex formation. Our data demonstrate that as well as a mechanism for regulating DNA binding, redox reactions can control replication by modulating the tertiary structure of critical protein factors using a specific redox sensor.

==About this Structure==

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[[Category: Bovine papillomavirus type 1]]

[[Category: Single protein]]

[[Category: Antson, A.A.]]

[[Category: Antson, A A.]]

[[Category: Ortiz-Lombardia, M.]]

[[Category: Sanders, C.M.]]

[[Category: Sanders, C M.]]

[[Category: Seavers, P.R.]]

[[Category: Seavers, P R.]]

[[Category: Sizov, D.]]

[[Category: activator]]

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[[Category: viral transcription factor]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:02:32 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-Redox changes are one of the factors that influence cell-cycle progression, and that control the processes of cellular proliferation, differentiation, senescence and apoptosis. Proteins regulated through redox-sensitive, cysteines have been characterized but specific 'sulphydryl switches' in, replication proteins remain to be identified. In bovine papillomavirus, type-1, DNA replication begins when the viral transcription factor E2, recruits the viral initiator protein E1 to the origin of DNA replication, (ori). Here we show that a novel dimerization interface in the E2, transcription activation domain is stabilized by a disulphide bond., Oxidative cross-linking via Cys57 sequesters the interaction surface, between E1 and E2, preventing pre-initiation and replication initiation, complex formation. Our data demonstrate that as well as a mechanism for, regulating DNA binding, redox reactions can control replication by, modulating the tertiary structure of critical protein factors using a, specific redox sensor.
+Redox changes are one of the factors that influence cell-cycle progression and that control the processes of cellular proliferation, differentiation, senescence and apoptosis. Proteins regulated through redox-sensitive cysteines have been characterized but specific 'sulphydryl switches' in replication proteins remain to be identified. In bovine papillomavirus type-1, DNA replication begins when the viral transcription factor E2 recruits the viral initiator protein E1 to the origin of DNA replication (ori). Here we show that a novel dimerization interface in the E2 transcription activation domain is stabilized by a disulphide bond. Oxidative cross-linking via Cys57 sequesters the interaction surface between E1 and E2, preventing pre-initiation and replication initiation complex formation. Our data demonstrate that as well as a mechanism for regulating DNA binding, redox reactions can control replication by modulating the tertiary structure of critical protein factors using a specific redox sensor.
 ==About this Structure==
@@ Line 13: / Line 13: @@
 [[Category: Bovine papillomavirus type 1]]
 [[Category: Single protein]]
-[[Category: Antson, A.A.]]
+[[Category: Antson, A A.]]
 [[Category: Ortiz-Lombardia, M.]]
-[[Category: Sanders, C.M.]]
+[[Category: Sanders, C M.]]
-[[Category: Seavers, P.R.]]
+[[Category: Seavers, P R.]]
 [[Category: Sizov, D.]]
 [[Category: activator]]
@@ Line 35: / Line 35: @@
 [[Category: viral transcription factor]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:47:33 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:02:32 2008''