Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase

Elizabeth R. Barry; Janet E. Lovett; Alessandro Costa; Susan M. Lea; Stephen D. Bell

doi:10.1073/pnas.0809192106

Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase

Elizabeth R. Barry, Janet E. Lovett, Alessandro Costa, Susan M. Lea, Stephen D. Bell^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

Abstract

The minichromosome maintenance (MCM) helicase is the presumptive replicative helicase in archaea and eukaryotes. The archaeal homomultimeric MCM has a two-tier structure. One tier contains the AAA+ motor domains of the proteins, and these are the minimal functional helicase domains. The second tier is formed by the N-terminal domains. These domains are not essential for MCM helicase activity but act to enhance the processivity of the helicase. We reveal that a conserved loop facilitates communication between processivity and motor tiers. Interestingly, this allostery seems to be mediated by interactions between, rather than within, individual protomers in the MCM ring.

Original language	English
Pages (from-to)	1051-1056
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	106
Issue number	4
DOIs	https://doi.org/10.1073/pnas.0809192106
Publication status	Published - 27 Jan 2009

Keywords

archaea
DNA replication
AAA plus protein
Sulfolobus
REPLICATIVE HEXAMERIC HELICASE
ARCHAEAL MCM
DNA
MECHANISM
PROTEIN
COMPLEX
TRANSLOCATION
DOMAINS

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10.1073/pnas.0809192106

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title = "Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase",

abstract = "The minichromosome maintenance (MCM) helicase is the presumptive replicative helicase in archaea and eukaryotes. The archaeal homomultimeric MCM has a two-tier structure. One tier contains the AAA+ motor domains of the proteins, and these are the minimal functional helicase domains. The second tier is formed by the N-terminal domains. These domains are not essential for MCM helicase activity but act to enhance the processivity of the helicase. We reveal that a conserved loop facilitates communication between processivity and motor tiers. Interestingly, this allostery seems to be mediated by interactions between, rather than within, individual protomers in the MCM ring.",

keywords = "archaea, DNA replication, AAA plus protein, Sulfolobus, REPLICATIVE HEXAMERIC HELICASE, ARCHAEAL MCM, DNA, MECHANISM, PROTEIN, COMPLEX, TRANSLOCATION, DOMAINS",

author = "Barry, \{Elizabeth R.\} and Lovett, \{Janet E.\} and Alessandro Costa and Lea, \{Susan M.\} and Bell, \{Stephen D.\}",

year = "2009",

month = jan,

day = "27",

doi = "10.1073/pnas.0809192106",

language = "English",

volume = "106",

pages = "1051--1056",

journal = "Proceedings of the National Academy of Sciences of the United States of America",

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publisher = "National Academy of Sciences",

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TY - JOUR

T1 - Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase

AU - Barry, Elizabeth R.

AU - Lovett, Janet E.

AU - Costa, Alessandro

AU - Lea, Susan M.

AU - Bell, Stephen D.

PY - 2009/1/27

Y1 - 2009/1/27

N2 - The minichromosome maintenance (MCM) helicase is the presumptive replicative helicase in archaea and eukaryotes. The archaeal homomultimeric MCM has a two-tier structure. One tier contains the AAA+ motor domains of the proteins, and these are the minimal functional helicase domains. The second tier is formed by the N-terminal domains. These domains are not essential for MCM helicase activity but act to enhance the processivity of the helicase. We reveal that a conserved loop facilitates communication between processivity and motor tiers. Interestingly, this allostery seems to be mediated by interactions between, rather than within, individual protomers in the MCM ring.

AB - The minichromosome maintenance (MCM) helicase is the presumptive replicative helicase in archaea and eukaryotes. The archaeal homomultimeric MCM has a two-tier structure. One tier contains the AAA+ motor domains of the proteins, and these are the minimal functional helicase domains. The second tier is formed by the N-terminal domains. These domains are not essential for MCM helicase activity but act to enhance the processivity of the helicase. We reveal that a conserved loop facilitates communication between processivity and motor tiers. Interestingly, this allostery seems to be mediated by interactions between, rather than within, individual protomers in the MCM ring.

KW - archaea

KW - DNA replication

KW - AAA plus protein

KW - Sulfolobus

KW - REPLICATIVE HEXAMERIC HELICASE

KW - ARCHAEAL MCM

KW - DNA

KW - MECHANISM

KW - PROTEIN

KW - COMPLEX

KW - TRANSLOCATION

KW - DOMAINS

UR - https://www.scopus.com/pages/publications/59049088137

U2 - 10.1073/pnas.0809192106

DO - 10.1073/pnas.0809192106

M3 - Article

SN - 0027-8424

VL - 106

SP - 1051

EP - 1056

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

IS - 4

ER -

Intersubunit allosteric communication mediated by a conserved loop in the MCM helicase

Abstract

Keywords

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