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Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins

The RecA family of proteins mediates homologous recombination, an evolutionarily conserved pathway that maintains genomic stability by protecting against DNA double strand breaks. RecA proteins are thought to facilitate DNA strand exchange reactions as closed-rings or as right-handed helical filamen...

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Autores principales: Chen, Li-Tzu, Ko, Tzu-Ping, Chang, Yuan-Chih, Lin, Kuei-An, Chang, Chia-Seng, Wang, Andrew H.-J., Wang, Ting-Fang
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2007
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1874592/
https://www.ncbi.nlm.nih.gov/pubmed/17329376
http://dx.doi.org/10.1093/nar/gkl1131
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author Chen, Li-Tzu
Ko, Tzu-Ping
Chang, Yuan-Chih
Lin, Kuei-An
Chang, Chia-Seng
Wang, Andrew H.-J.
Wang, Ting-Fang
author_facet Chen, Li-Tzu
Ko, Tzu-Ping
Chang, Yuan-Chih
Lin, Kuei-An
Chang, Chia-Seng
Wang, Andrew H.-J.
Wang, Ting-Fang
author_sort Chen, Li-Tzu
collection PubMed
description The RecA family of proteins mediates homologous recombination, an evolutionarily conserved pathway that maintains genomic stability by protecting against DNA double strand breaks. RecA proteins are thought to facilitate DNA strand exchange reactions as closed-rings or as right-handed helical filaments. Here, we report the crystal structure of a left-handed Sulfolobus solfataricus RadA helical filament. Each protomer in this left-handed filament is linked to its neighbour via interactions of a β-strand polymerization motif with the neighbouring ATPase domain. Immediately following the polymerization motif, we identified an evolutionarily conserved hinge region (a subunit rotation motif) in which a 360° clockwise axial rotation accompanies stepwise structural transitions from a closed ring to the AMP–PNP right-handed filament, then to an overwound right-handed filament and finally to the left-handed filament. Additional structural and functional analyses of wild-type and mutant proteins confirmed that the subunit rotation motif is crucial for enzymatic functions of RecA family proteins. These observations support the hypothesis that RecA family protein filaments may function as rotary motors.
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spelling pubmed-18745922007-05-23 Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins Chen, Li-Tzu Ko, Tzu-Ping Chang, Yuan-Chih Lin, Kuei-An Chang, Chia-Seng Wang, Andrew H.-J. Wang, Ting-Fang Nucleic Acids Res Structural Biology The RecA family of proteins mediates homologous recombination, an evolutionarily conserved pathway that maintains genomic stability by protecting against DNA double strand breaks. RecA proteins are thought to facilitate DNA strand exchange reactions as closed-rings or as right-handed helical filaments. Here, we report the crystal structure of a left-handed Sulfolobus solfataricus RadA helical filament. Each protomer in this left-handed filament is linked to its neighbour via interactions of a β-strand polymerization motif with the neighbouring ATPase domain. Immediately following the polymerization motif, we identified an evolutionarily conserved hinge region (a subunit rotation motif) in which a 360° clockwise axial rotation accompanies stepwise structural transitions from a closed ring to the AMP–PNP right-handed filament, then to an overwound right-handed filament and finally to the left-handed filament. Additional structural and functional analyses of wild-type and mutant proteins confirmed that the subunit rotation motif is crucial for enzymatic functions of RecA family proteins. These observations support the hypothesis that RecA family protein filaments may function as rotary motors. Oxford University Press 2007-03 2007-02-28 /pmc/articles/PMC1874592/ /pubmed/17329376 http://dx.doi.org/10.1093/nar/gkl1131 Text en © 2007 The Author(s) This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Structural Biology
Chen, Li-Tzu
Ko, Tzu-Ping
Chang, Yuan-Chih
Lin, Kuei-An
Chang, Chia-Seng
Wang, Andrew H.-J.
Wang, Ting-Fang
Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins
title Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins
title_full Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins
title_fullStr Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins
title_full_unstemmed Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins
title_short Crystal structure of the left-handed archaeal RadA helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of RecA family proteins
title_sort crystal structure of the left-handed archaeal rada helical filament: identification of a functional motif for controlling quaternary structures and enzymatic functions of reca family proteins
topic Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1874592/
https://www.ncbi.nlm.nih.gov/pubmed/17329376
http://dx.doi.org/10.1093/nar/gkl1131
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