Sulfolobus Replication Factor C stimulates the activity of DNA Polymerase B1

Xuanxuan Xing; Likui Zhang; Li Guo; Qunxin She; Li Huang

doi:10.1128/JB.01552-14

Sulfolobus Replication Factor C stimulates the activity of DNA Polymerase B1

Xuanxuan Xing, Likui Zhang, Li Guo, Qunxin She, Li Huang

Functional genomics

4 Citationer (Scopus)

Abstract

Replication factor C (RFC) is known to function in loading proliferating cell nuclear antigen (PCNA) onto primed DNA, allowing PCNA to tether DNA polymerase for highly processive DNA synthesis in eukaryotic and archaeal replication. In this report, we show that an RFC complex from the hyperthermophilic archaea of the genus Sulfolobus physically interacts with DNA polymerase B1 (PolB1) and enhances both the polymerase and 3'-5' exonuclease activities of PolB1 in an ATP-independent manner. Stimulation of the PolB1 activity by RFC is independent of the ability of RFC to bind DNA but is consistent with the ability of RFC to facilitate DNA binding by PolB1 through protein-protein interaction. These results suggest that Sulfolobus RFC may play a role in recruiting DNA polymerase for efficient primer extension, in addition to clamp loading, during DNA replication.

Originalsprog	Engelsk
Tidsskrift	Journal of Bacteriology
Vol/bind	196
Udgave nummer	13
Sider (fra-til)	2367-2375
Antal sider	9
ISSN	0021-9193
DOI	https://doi.org/10.1128/JB.01552-14
Status	Udgivet - 2014

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10.1128/JB.01552-14

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title = "Sulfolobus Replication Factor C stimulates the activity of DNA Polymerase B1",

abstract = "Replication factor C (RFC) is known to function in loading proliferating cell nuclear antigen (PCNA) onto primed DNA, allowing PCNA to tether DNA polymerase for highly processive DNA synthesis in eukaryotic and archaeal replication. In this report, we show that an RFC complex from the hyperthermophilic archaea of the genus Sulfolobus physically interacts with DNA polymerase B1 (PolB1) and enhances both the polymerase and 3'-5' exonuclease activities of PolB1 in an ATP-independent manner. Stimulation of the PolB1 activity by RFC is independent of the ability of RFC to bind DNA but is consistent with the ability of RFC to facilitate DNA binding by PolB1 through protein-protein interaction. These results suggest that Sulfolobus RFC may play a role in recruiting DNA polymerase for efficient primer extension, in addition to clamp loading, during DNA replication.",

author = "Xuanxuan Xing and Likui Zhang and Li Guo and Qunxin She and Li Huang",

year = "2014",

doi = "10.1128/JB.01552-14",

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T1 - Sulfolobus Replication Factor C stimulates the activity of DNA Polymerase B1

AU - Xing, Xuanxuan

AU - Zhang, Likui

AU - Guo, Li

AU - She, Qunxin

AU - Huang, Li

PY - 2014

Y1 - 2014

N2 - Replication factor C (RFC) is known to function in loading proliferating cell nuclear antigen (PCNA) onto primed DNA, allowing PCNA to tether DNA polymerase for highly processive DNA synthesis in eukaryotic and archaeal replication. In this report, we show that an RFC complex from the hyperthermophilic archaea of the genus Sulfolobus physically interacts with DNA polymerase B1 (PolB1) and enhances both the polymerase and 3'-5' exonuclease activities of PolB1 in an ATP-independent manner. Stimulation of the PolB1 activity by RFC is independent of the ability of RFC to bind DNA but is consistent with the ability of RFC to facilitate DNA binding by PolB1 through protein-protein interaction. These results suggest that Sulfolobus RFC may play a role in recruiting DNA polymerase for efficient primer extension, in addition to clamp loading, during DNA replication.

AB - Replication factor C (RFC) is known to function in loading proliferating cell nuclear antigen (PCNA) onto primed DNA, allowing PCNA to tether DNA polymerase for highly processive DNA synthesis in eukaryotic and archaeal replication. In this report, we show that an RFC complex from the hyperthermophilic archaea of the genus Sulfolobus physically interacts with DNA polymerase B1 (PolB1) and enhances both the polymerase and 3'-5' exonuclease activities of PolB1 in an ATP-independent manner. Stimulation of the PolB1 activity by RFC is independent of the ability of RFC to bind DNA but is consistent with the ability of RFC to facilitate DNA binding by PolB1 through protein-protein interaction. These results suggest that Sulfolobus RFC may play a role in recruiting DNA polymerase for efficient primer extension, in addition to clamp loading, during DNA replication.

U2 - 10.1128/JB.01552-14

DO - 10.1128/JB.01552-14

M3 - Journal article

C2 - 24748616

SN - 0021-9193

VL - 196

SP - 2367

EP - 2375

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 13

ER -

Sulfolobus Replication Factor C stimulates the activity of DNA Polymerase B1

Abstract

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