The accessibility of DNA to dimethylsulfate in complexes with recA protein.

Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA...
Ausführliche Beschreibung

Gespeichert in:

Autor*in:	Di Capua, E. [verfasserIn] Müller, B. [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	1987

Anmerkung:	© European Molecular Biology Organization 1987

Übergeordnetes Werk:	Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 6(1987), 8 vom: 01. Aug., Seite 2493-2498
Übergeordnetes Werk:	volume:6 ; year:1987 ; number:8 ; day:01 ; month:08 ; pages:2493-2498

Links:	Volltext

DOI / URN:	10.1002/j.1460-2075.1987.tb02531.x

Katalog-ID:	SPR057567166

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245	1	0	\|a The accessibility of DNA to dimethylsulfate in complexes with recA protein.
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520			\|a Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA helix, to which it imparts a new helicity of 18.5 bp per turn of 97 A pitch. Here we test the accessibility of the DNA in the complex to modification by dimethylsulfate, and find that the complexed DNA is approximately 2‐fold more reactive on the major groove side than it was in B‐DNA (methylation of guanine N7), while it is protected approximately 2‐fold on the minor groove side (methylation of adenine N3), suggesting that the protein coats the DNA along the minor groove. Furthermore, N3 of cytosine, a residue involved in base pairing, is found exposed in complexes with single strands as it is in naked single‐stranded DNA, while it remains inaccessible in complexes with double strands, suggesting that the latter is not melted at this stage of the strand exchange reaction.
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allfields	10.1002/j.1460-2075.1987.tb02531.x doi (DE-627)SPR057567166 (SPR)j.1460-2075.1987.tb02531.x-e DE-627 ger DE-627 rakwb eng Di Capua, E. verfasserin aut The accessibility of DNA to dimethylsulfate in complexes with recA protein. 1987 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1987 Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA helix, to which it imparts a new helicity of 18.5 bp per turn of 97 A pitch. Here we test the accessibility of the DNA in the complex to modification by dimethylsulfate, and find that the complexed DNA is approximately 2‐fold more reactive on the major groove side than it was in B‐DNA (methylation of guanine N7), while it is protected approximately 2‐fold on the minor groove side (methylation of adenine N3), suggesting that the protein coats the DNA along the minor groove. Furthermore, N3 of cytosine, a residue involved in base pairing, is found exposed in complexes with single strands as it is in naked single‐stranded DNA, while it remains inaccessible in complexes with double strands, suggesting that the latter is not melted at this stage of the strand exchange reaction. Müller, B. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 6(1987), 8 vom: 01. Aug., Seite 2493-2498 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:6 year:1987 number:8 day:01 month:08 pages:2493-2498 https://dx.doi.org/10.1002/j.1460-2075.1987.tb02531.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 1987 8 01 08 2493-2498
spelling	10.1002/j.1460-2075.1987.tb02531.x doi (DE-627)SPR057567166 (SPR)j.1460-2075.1987.tb02531.x-e DE-627 ger DE-627 rakwb eng Di Capua, E. verfasserin aut The accessibility of DNA to dimethylsulfate in complexes with recA protein. 1987 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1987 Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA helix, to which it imparts a new helicity of 18.5 bp per turn of 97 A pitch. Here we test the accessibility of the DNA in the complex to modification by dimethylsulfate, and find that the complexed DNA is approximately 2‐fold more reactive on the major groove side than it was in B‐DNA (methylation of guanine N7), while it is protected approximately 2‐fold on the minor groove side (methylation of adenine N3), suggesting that the protein coats the DNA along the minor groove. Furthermore, N3 of cytosine, a residue involved in base pairing, is found exposed in complexes with single strands as it is in naked single‐stranded DNA, while it remains inaccessible in complexes with double strands, suggesting that the latter is not melted at this stage of the strand exchange reaction. Müller, B. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 6(1987), 8 vom: 01. Aug., Seite 2493-2498 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:6 year:1987 number:8 day:01 month:08 pages:2493-2498 https://dx.doi.org/10.1002/j.1460-2075.1987.tb02531.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 1987 8 01 08 2493-2498
allfields_unstemmed	10.1002/j.1460-2075.1987.tb02531.x doi (DE-627)SPR057567166 (SPR)j.1460-2075.1987.tb02531.x-e DE-627 ger DE-627 rakwb eng Di Capua, E. verfasserin aut The accessibility of DNA to dimethylsulfate in complexes with recA protein. 1987 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1987 Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA helix, to which it imparts a new helicity of 18.5 bp per turn of 97 A pitch. Here we test the accessibility of the DNA in the complex to modification by dimethylsulfate, and find that the complexed DNA is approximately 2‐fold more reactive on the major groove side than it was in B‐DNA (methylation of guanine N7), while it is protected approximately 2‐fold on the minor groove side (methylation of adenine N3), suggesting that the protein coats the DNA along the minor groove. Furthermore, N3 of cytosine, a residue involved in base pairing, is found exposed in complexes with single strands as it is in naked single‐stranded DNA, while it remains inaccessible in complexes with double strands, suggesting that the latter is not melted at this stage of the strand exchange reaction. Müller, B. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 6(1987), 8 vom: 01. Aug., Seite 2493-2498 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:6 year:1987 number:8 day:01 month:08 pages:2493-2498 https://dx.doi.org/10.1002/j.1460-2075.1987.tb02531.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 1987 8 01 08 2493-2498
allfieldsGer	10.1002/j.1460-2075.1987.tb02531.x doi (DE-627)SPR057567166 (SPR)j.1460-2075.1987.tb02531.x-e DE-627 ger DE-627 rakwb eng Di Capua, E. verfasserin aut The accessibility of DNA to dimethylsulfate in complexes with recA protein. 1987 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1987 Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA helix, to which it imparts a new helicity of 18.5 bp per turn of 97 A pitch. Here we test the accessibility of the DNA in the complex to modification by dimethylsulfate, and find that the complexed DNA is approximately 2‐fold more reactive on the major groove side than it was in B‐DNA (methylation of guanine N7), while it is protected approximately 2‐fold on the minor groove side (methylation of adenine N3), suggesting that the protein coats the DNA along the minor groove. Furthermore, N3 of cytosine, a residue involved in base pairing, is found exposed in complexes with single strands as it is in naked single‐stranded DNA, while it remains inaccessible in complexes with double strands, suggesting that the latter is not melted at this stage of the strand exchange reaction. Müller, B. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 6(1987), 8 vom: 01. Aug., Seite 2493-2498 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:6 year:1987 number:8 day:01 month:08 pages:2493-2498 https://dx.doi.org/10.1002/j.1460-2075.1987.tb02531.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 1987 8 01 08 2493-2498
allfieldsSound	10.1002/j.1460-2075.1987.tb02531.x doi (DE-627)SPR057567166 (SPR)j.1460-2075.1987.tb02531.x-e DE-627 ger DE-627 rakwb eng Di Capua, E. verfasserin aut The accessibility of DNA to dimethylsulfate in complexes with recA protein. 1987 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1987 Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA helix, to which it imparts a new helicity of 18.5 bp per turn of 97 A pitch. Here we test the accessibility of the DNA in the complex to modification by dimethylsulfate, and find that the complexed DNA is approximately 2‐fold more reactive on the major groove side than it was in B‐DNA (methylation of guanine N7), while it is protected approximately 2‐fold on the minor groove side (methylation of adenine N3), suggesting that the protein coats the DNA along the minor groove. Furthermore, N3 of cytosine, a residue involved in base pairing, is found exposed in complexes with single strands as it is in naked single‐stranded DNA, while it remains inaccessible in complexes with double strands, suggesting that the latter is not melted at this stage of the strand exchange reaction. Müller, B. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 6(1987), 8 vom: 01. Aug., Seite 2493-2498 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:6 year:1987 number:8 day:01 month:08 pages:2493-2498 https://dx.doi.org/10.1002/j.1460-2075.1987.tb02531.x X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_213 GBV_ILN_230 GBV_ILN_252 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2014 GBV_ILN_2021 GBV_ILN_2050 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 6 1987 8 01 08 2493-2498
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author	Di Capua, E.
spellingShingle	Di Capua, E. The accessibility of DNA to dimethylsulfate in complexes with recA protein.
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topic_title	The accessibility of DNA to dimethylsulfate in complexes with recA protein
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title	The accessibility of DNA to dimethylsulfate in complexes with recA protein.
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title_full	The accessibility of DNA to dimethylsulfate in complexes with recA protein
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title_sort	the accessibility of dna to dimethylsulfate in complexes with reca protein
title_auth	The accessibility of DNA to dimethylsulfate in complexes with recA protein.
abstract	Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA helix, to which it imparts a new helicity of 18.5 bp per turn of 97 A pitch. Here we test the accessibility of the DNA in the complex to modification by dimethylsulfate, and find that the complexed DNA is approximately 2‐fold more reactive on the major groove side than it was in B‐DNA (methylation of guanine N7), while it is protected approximately 2‐fold on the minor groove side (methylation of adenine N3), suggesting that the protein coats the DNA along the minor groove. Furthermore, N3 of cytosine, a residue involved in base pairing, is found exposed in complexes with single strands as it is in naked single‐stranded DNA, while it remains inaccessible in complexes with double strands, suggesting that the latter is not melted at this stage of the strand exchange reaction. © European Molecular Biology Organization 1987
abstractGer	Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA helix, to which it imparts a new helicity of 18.5 bp per turn of 97 A pitch. Here we test the accessibility of the DNA in the complex to modification by dimethylsulfate, and find that the complexed DNA is approximately 2‐fold more reactive on the major groove side than it was in B‐DNA (methylation of guanine N7), while it is protected approximately 2‐fold on the minor groove side (methylation of adenine N3), suggesting that the protein coats the DNA along the minor groove. Furthermore, N3 of cytosine, a residue involved in base pairing, is found exposed in complexes with single strands as it is in naked single‐stranded DNA, while it remains inaccessible in complexes with double strands, suggesting that the latter is not melted at this stage of the strand exchange reaction. © European Molecular Biology Organization 1987
abstract_unstemmed	Abstract recA protein coats DNA co‐operatively to form filaments approximately 100 A thick, which in the presence of ATP, and more stably so in the presence of the non‐hydrolyzable analog ATP gamma S, have a helical appearance with a deep cleft in the protein coat. This protein helix follows the DNA helix, to which it imparts a new helicity of 18.5 bp per turn of 97 A pitch. Here we test the accessibility of the DNA in the complex to modification by dimethylsulfate, and find that the complexed DNA is approximately 2‐fold more reactive on the major groove side than it was in B‐DNA (methylation of guanine N7), while it is protected approximately 2‐fold on the minor groove side (methylation of adenine N3), suggesting that the protein coats the DNA along the minor groove. Furthermore, N3 of cytosine, a residue involved in base pairing, is found exposed in complexes with single strands as it is in naked single‐stranded DNA, while it remains inaccessible in complexes with double strands, suggesting that the latter is not melted at this stage of the strand exchange reaction. © European Molecular Biology Organization 1987
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title_short	The accessibility of DNA to dimethylsulfate in complexes with recA protein.
url	https://dx.doi.org/10.1002/j.1460-2075.1987.tb02531.x
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