Holliday junction branch migration driven by AAA+ ATPase motors

Jiri Wald; Thomas C Marlovits

doi:10.1016/j.sbi.2023.102650

Holliday junction branch migration driven by AAA+ ATPase motors

Standard

Holliday junction branch migration driven by AAA+ ATPase motors. / Wald, Jiri ; Marlovits, Thomas C.

In: CURR OPIN STRUC BIOL, Vol. 82, 10.2023, p. 102650.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Wald, J & Marlovits, TC 2023, 'Holliday junction branch migration driven by AAA+ ATPase motors', CURR OPIN STRUC BIOL, vol. 82, pp. 102650. https://doi.org/10.1016/j.sbi.2023.102650

APA

Wald, J., & Marlovits, T. C. (2023). Holliday junction branch migration driven by AAA+ ATPase motors. CURR OPIN STRUC BIOL, 82, 102650. https://doi.org/10.1016/j.sbi.2023.102650

Vancouver

Wald J , Marlovits TC. Holliday junction branch migration driven by AAA+ ATPase motors. CURR OPIN STRUC BIOL. 2023 Oct;82:102650. https://doi.org/10.1016/j.sbi.2023.102650

Bibtex

@article{7e71f39c95724724be8286e8bf649ae4,

title = "Holliday junction branch migration driven by AAA+ ATPase motors",

abstract = "Holliday junctions are key intermediate DNA structures during genetic recombination. One of the first Holliday junction-processing protein complexes to be discovered was the well conserved RuvAB branch migration complex present in bacteria that mediates an ATP-dependent movement of the Holliday junction (branch migration). Although the RuvAB complex served as a paradigm for the processing of the Holliday junction, due to technical limitations the detailed structure and underlying mechanism of the RuvAB branch migration complex has until now remained unclear. Recently, structures of a reconstituted RuvAB complex actively-processing a Holliday junction were resolved using time-resolved cryo-electron microscopy. These structures showed distinct conformational states at different stages of the migration process. These structures made it possible to propose an integrated model for RuvAB Holliday junction branch migration. Furthermore, they revealed unexpected insights into the highly coordinated and regulated mechanisms of the nucleotide cycle powering substrate translocation in the hexameric AAA+ RuvB ATPase. Here, we review these latest advances and describe areas for future research.",

keywords = "DNA, Cruciform, Cryoelectron Microscopy, ATPases Associated with Diverse Cellular Activities, Movement, Nucleotides",

author = "Jiri Wald and Marlovits, {Thomas C}",

note = "Copyright {\textcopyright} 2023. Published by Elsevier Ltd.",

year = "2023",

month = oct,

doi = "10.1016/j.sbi.2023.102650",

language = "English",

volume = "82",

pages = "102650",

journal = "CURR OPIN STRUC BIOL",

issn = "0959-440X",

publisher = "Elsevier Limited",

}

RIS

TY - JOUR

T1 - Holliday junction branch migration driven by AAA+ ATPase motors

AU - Wald, Jiri

AU - Marlovits, Thomas C

PY - 2023/10

Y1 - 2023/10

N2 - Holliday junctions are key intermediate DNA structures during genetic recombination. One of the first Holliday junction-processing protein complexes to be discovered was the well conserved RuvAB branch migration complex present in bacteria that mediates an ATP-dependent movement of the Holliday junction (branch migration). Although the RuvAB complex served as a paradigm for the processing of the Holliday junction, due to technical limitations the detailed structure and underlying mechanism of the RuvAB branch migration complex has until now remained unclear. Recently, structures of a reconstituted RuvAB complex actively-processing a Holliday junction were resolved using time-resolved cryo-electron microscopy. These structures showed distinct conformational states at different stages of the migration process. These structures made it possible to propose an integrated model for RuvAB Holliday junction branch migration. Furthermore, they revealed unexpected insights into the highly coordinated and regulated mechanisms of the nucleotide cycle powering substrate translocation in the hexameric AAA+ RuvB ATPase. Here, we review these latest advances and describe areas for future research.

AB - Holliday junctions are key intermediate DNA structures during genetic recombination. One of the first Holliday junction-processing protein complexes to be discovered was the well conserved RuvAB branch migration complex present in bacteria that mediates an ATP-dependent movement of the Holliday junction (branch migration). Although the RuvAB complex served as a paradigm for the processing of the Holliday junction, due to technical limitations the detailed structure and underlying mechanism of the RuvAB branch migration complex has until now remained unclear. Recently, structures of a reconstituted RuvAB complex actively-processing a Holliday junction were resolved using time-resolved cryo-electron microscopy. These structures showed distinct conformational states at different stages of the migration process. These structures made it possible to propose an integrated model for RuvAB Holliday junction branch migration. Furthermore, they revealed unexpected insights into the highly coordinated and regulated mechanisms of the nucleotide cycle powering substrate translocation in the hexameric AAA+ RuvB ATPase. Here, we review these latest advances and describe areas for future research.

KW - DNA, Cruciform

KW - Cryoelectron Microscopy

KW - ATPases Associated with Diverse Cellular Activities

KW - Movement

KW - Nucleotides

U2 - 10.1016/j.sbi.2023.102650

DO - 10.1016/j.sbi.2023.102650

M3 - SCORING: Review article

C2 - 37604043

VL - 82

SP - 102650

JO - CURR OPIN STRUC BIOL

JF - CURR OPIN STRUC BIOL

SN - 0959-440X

ER -