Strand invasion by HLTF as a mechanism for template switch in
fork rescue

J 2014

Strand invasion by HLTF as a mechanism for template switch in fork rescue

BURKOVICS, Peter, Marek ŠEBESTA, David BALOGH, Lajos HARACSKA, Lumír KREJČÍ et. al.

Basic information

Original name

Strand invasion by HLTF as a mechanism for template switch in fork rescue

Authors

BURKOVICS, Peter (348 Hungary, belonging to the institution), Marek ŠEBESTA (703 Slovakia, belonging to the institution), David BALOGH (348 Hungary), Lajos HARACSKA (348 Hungary) and Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution)

Edition

Nucleic Acids Research, Oxford, Oxford University Press, 2014, 0305-1048

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

Genetics and molecular biology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 9.112

RIV identification code

RIV/00216224:14110/14:00073467

Organization unit

Faculty of Medicine

DOI

http://dx.doi.org/10.1093/nar/gkt1040

UT WoS

000331138800030

Keywords in English

TRANSLESION DNA-SYNTHESIS; CELL NUCLEAR ANTIGEN; HOMOLOGOUS RECOMBINATION; POSTREPLICATION REPAIR; SACCHAROMYCES-CEREVISIAE; REPLICATION FORK; DAMAGED DNA; UBIQUITIN LIGASE; POLYMERASE IOTA; RAD51 PROTEIN

Abstract

V originále

Stalling of replication forks at unrepaired DNA lesions can result in discontinuities opposite the damage in the newly synthesized DNA strand. Translesion synthesis or facilitating the copy from the newly synthesized strand of the sister duplex by template switching can overcome such discontinuities. During template switch, a new primer–template junction has to be formed and two mechanisms, including replication fork reversal and D-loop formation have been suggested. Genetic evidence indicates a major role for yeast Rad5 in template switch and that both Rad5 and its human orthologue, Helicase-like transcription factor (HLTF), a potential tumour suppressor can facilitate replication fork reversal. This study demonstrates the ability of HLTF and Rad5 to form a D-loop without requiring ATP binding and/or hydrolysis. We also show that this strand-pairing activity is independent of RAD51 in vitro and is not mechanistically related to that of another member of the SWI/SNF family, RAD54. In addition, the 30-end of the invading strand in the D-loop can serve as a primer and is extended by DNA polymerase. Our data indicate that HLTF is involved in a RAD51-independent Dloop branch of template switch pathway that can promote repair of gaps formed during replication of damaged DNA.

Links

EE2.3.20.0011, research and development project

Name: Centrum výzkumu pluripotentních buněk a nestability genomu

GAP207/12/2323, research and development project

Name: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I

Investor: Czech Science Foundation

GA13-26629S, research and development project

Name: SUMO a stability genomu

Investor: Czech Science Foundation

Citovat

BURKOVICS, Peter, Marek ŠEBESTA, David BALOGH, Lajos HARACSKA and Lumír KREJČÍ. Strand invasion by HLTF as a mechanism for template switch in fork rescue. Nucleic Acids Research. Oxford: Oxford University Press, 2014, vol. 42, No 3, p. 1711-1720. ISSN 0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkt1040.

@article{1160748,
   author = {Burkovics, Peter and Šebesta, Marek and Balogh, David and Haracska, Lajos and Krejčí, Lumír},
   article_location = {Oxford},
   article_number = {3},
   doi = {http://dx.doi.org/10.1093/nar/gkt1040},
   keywords = {TRANSLESION DNA-SYNTHESIS; CELL NUCLEAR ANTIGEN; HOMOLOGOUS RECOMBINATION; POSTREPLICATION REPAIR; SACCHAROMYCES-CEREVISIAE; REPLICATION FORK; DAMAGED DNA; UBIQUITIN LIGASE; POLYMERASE IOTA; RAD51 PROTEIN},
   language = {eng},
   issn = {0305-1048},
   journal = {Nucleic Acids Research},
   title = {Strand invasion by HLTF as a mechanism for template switch in fork rescue},
   volume = {42},
   year = {2014}
}

TY  - JOUR
ID  - 1160748
AU  - Burkovics, Peter - Šebesta, Marek - Balogh, David - Haracska, Lajos - Krejčí, Lumír
PY  - 2014
TI  - Strand invasion by HLTF as a mechanism for template switch in fork rescue
JF  - Nucleic Acids Research
VL  - 42
IS  - 3
SP  - 1711-1720
EP  - 1711-1720
PB  - Oxford University Press
SN  - 03051048
KW  - TRANSLESION DNA-SYNTHESIS
KW  - CELL NUCLEAR ANTIGEN
KW  - HOMOLOGOUS RECOMBINATION
KW  - POSTREPLICATION REPAIR
KW  - SACCHAROMYCES-CEREVISIAE
KW  - REPLICATION FORK
KW  - DAMAGED DNA
KW  - UBIQUITIN LIGASE
KW  - POLYMERASE IOTA
KW  - RAD51 PROTEIN
N2  - Stalling of replication forks at unrepaired DNA lesions can result in discontinuities opposite the damage in the newly synthesized DNA strand. Translesion synthesis or facilitating the copy from the newly synthesized strand of the sister duplex by template switching can overcome such discontinuities. During template switch, a new primer–template junction has to be formed and two mechanisms, including replication fork reversal and D-loop formation have been suggested. Genetic evidence indicates a major role for yeast Rad5 in template switch and that both Rad5 and its human orthologue, Helicase-like transcription factor (HLTF), a potential tumour suppressor can facilitate replication fork reversal. This study demonstrates the ability of HLTF and Rad5 to form a D-loop without requiring ATP binding and/or hydrolysis. We also show that this strand-pairing activity is independent of RAD51 in vitro and is not mechanistically related to that of another member of the SWI/SNF family, RAD54. In addition, the 30-end of the invading strand in the D-loop can serve as a primer and is extended by DNA polymerase. Our data indicate that HLTF is involved in a RAD51-independent Dloop branch of template switch pathway that can promote repair of gaps formed during replication of damaged DNA.
ER  -

BURKOVICS, Peter, Marek ŠEBESTA, David BALOGH, Lajos HARACSKA and Lumír KREJČÍ. Strand invasion by HLTF as a mechanism for template switch in fork rescue. \textit{Nucleic Acids Research}. Oxford: Oxford University Press, 2014, vol.~42, No~3, p.~1711-1720. ISSN~0305-1048. Available from: https://dx.doi.org/10.1093/nar/gkt1040.

Detailed Information on Publication Record