Differential arrangements of conserved building blocks among homologs of the Rad50/Mre11 DNA repair protein complex

Martijn De Jager, Kelly M. Trujillo, Patrick Sung, Karl Peter Hopfner, James P. Carney, John A. Tainer, John C. Connelly, David R.F. Leach, Roland Kanaar, Claire Wyman

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

Structural maintenance of chromosomes (SMC) proteins have diverse cellular functions including chromosome segregation, condensation and DNA repair. They are grouped based on a conserved set of distinct structural motifs. All SMC proteins are predicted to have a bipartite ATPase domain that is separated by a long region predicted to form a coiled coil. Recent structural data on a variety of SMC proteins shows them to be arranged as long intramolecular coiled coils with a globular ATPase at one end. SMC proteins function in pairs as heterodimers or as homodimers often in complexes with other proteins. We expect the arrangement of the SMC protein domains in complex assemblies to have important implications for their diverse functions. We used scanning force microscopy imaging to determine the architecture of human, Saccharomyces cerevisiae, and Pyrococcus furiosus Rad50/Mre11, Escherichia coli SbcCD, and S.cerevisiae SMC1/SMC3 cohesin SMC complexes. Two distinct architectural arrangements are described, based on the way their components were connected. The eukaryotic complexes were similar to each other and differed from their prokaryotic and archaeal homologs. These similarities and differences are discussed with respect to their diverse mechanistic roles in chromosome metabolism.

Original languageEnglish (US)
Pages (from-to)937-949
Number of pages13
JournalJournal of Molecular Biology
Volume339
Issue number4
DOIs
StatePublished - Jun 11 2004

Fingerprint

DNA Repair
Chromosomes
Maintenance
Proteins
Saccharomyces cerevisiae
Adenosine Triphosphatases
Pyrococcus furiosus
Chromosome Segregation
Atomic Force Microscopy
Escherichia coli

Keywords

  • DNA metabolism
  • SFM, scanning force microscopy
  • SMC, structural maintenance of chromosomes
  • SbcCD
  • protein architecture
  • scanning force microscopy (SFM)
  • structural maintenance of chromosomes (SMC)

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

De Jager, M., Trujillo, K. M., Sung, P., Hopfner, K. P., Carney, J. P., Tainer, J. A., ... Wyman, C. (2004). Differential arrangements of conserved building blocks among homologs of the Rad50/Mre11 DNA repair protein complex. Journal of Molecular Biology, 339(4), 937-949. https://doi.org/10.1016/j.jmb.2004.04.014

Differential arrangements of conserved building blocks among homologs of the Rad50/Mre11 DNA repair protein complex. / De Jager, Martijn; Trujillo, Kelly M.; Sung, Patrick; Hopfner, Karl Peter; Carney, James P.; Tainer, John A.; Connelly, John C.; Leach, David R.F.; Kanaar, Roland; Wyman, Claire.

In: Journal of Molecular Biology, Vol. 339, No. 4, 11.06.2004, p. 937-949.

Research output: Contribution to journalArticle

De Jager, M, Trujillo, KM, Sung, P, Hopfner, KP, Carney, JP, Tainer, JA, Connelly, JC, Leach, DRF, Kanaar, R & Wyman, C 2004, 'Differential arrangements of conserved building blocks among homologs of the Rad50/Mre11 DNA repair protein complex', Journal of Molecular Biology, vol. 339, no. 4, pp. 937-949. https://doi.org/10.1016/j.jmb.2004.04.014
De Jager, Martijn ; Trujillo, Kelly M. ; Sung, Patrick ; Hopfner, Karl Peter ; Carney, James P. ; Tainer, John A. ; Connelly, John C. ; Leach, David R.F. ; Kanaar, Roland ; Wyman, Claire. / Differential arrangements of conserved building blocks among homologs of the Rad50/Mre11 DNA repair protein complex. In: Journal of Molecular Biology. 2004 ; Vol. 339, No. 4. pp. 937-949.
@article{947056ff2dcc40399ccd065e1227bfc3,
title = "Differential arrangements of conserved building blocks among homologs of the Rad50/Mre11 DNA repair protein complex",
abstract = "Structural maintenance of chromosomes (SMC) proteins have diverse cellular functions including chromosome segregation, condensation and DNA repair. They are grouped based on a conserved set of distinct structural motifs. All SMC proteins are predicted to have a bipartite ATPase domain that is separated by a long region predicted to form a coiled coil. Recent structural data on a variety of SMC proteins shows them to be arranged as long intramolecular coiled coils with a globular ATPase at one end. SMC proteins function in pairs as heterodimers or as homodimers often in complexes with other proteins. We expect the arrangement of the SMC protein domains in complex assemblies to have important implications for their diverse functions. We used scanning force microscopy imaging to determine the architecture of human, Saccharomyces cerevisiae, and Pyrococcus furiosus Rad50/Mre11, Escherichia coli SbcCD, and S.cerevisiae SMC1/SMC3 cohesin SMC complexes. Two distinct architectural arrangements are described, based on the way their components were connected. The eukaryotic complexes were similar to each other and differed from their prokaryotic and archaeal homologs. These similarities and differences are discussed with respect to their diverse mechanistic roles in chromosome metabolism.",
keywords = "DNA metabolism, SFM, scanning force microscopy, SMC, structural maintenance of chromosomes, SbcCD, protein architecture, scanning force microscopy (SFM), structural maintenance of chromosomes (SMC)",
author = "{De Jager}, Martijn and Trujillo, {Kelly M.} and Patrick Sung and Hopfner, {Karl Peter} and Carney, {James P.} and Tainer, {John A.} and Connelly, {John C.} and Leach, {David R.F.} and Roland Kanaar and Claire Wyman",
year = "2004",
month = "6",
day = "11",
doi = "10.1016/j.jmb.2004.04.014",
language = "English (US)",
volume = "339",
pages = "937--949",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "4",

}

TY - JOUR

T1 - Differential arrangements of conserved building blocks among homologs of the Rad50/Mre11 DNA repair protein complex

AU - De Jager, Martijn

AU - Trujillo, Kelly M.

AU - Sung, Patrick

AU - Hopfner, Karl Peter

AU - Carney, James P.

AU - Tainer, John A.

AU - Connelly, John C.

AU - Leach, David R.F.

AU - Kanaar, Roland

AU - Wyman, Claire

PY - 2004/6/11

Y1 - 2004/6/11

N2 - Structural maintenance of chromosomes (SMC) proteins have diverse cellular functions including chromosome segregation, condensation and DNA repair. They are grouped based on a conserved set of distinct structural motifs. All SMC proteins are predicted to have a bipartite ATPase domain that is separated by a long region predicted to form a coiled coil. Recent structural data on a variety of SMC proteins shows them to be arranged as long intramolecular coiled coils with a globular ATPase at one end. SMC proteins function in pairs as heterodimers or as homodimers often in complexes with other proteins. We expect the arrangement of the SMC protein domains in complex assemblies to have important implications for their diverse functions. We used scanning force microscopy imaging to determine the architecture of human, Saccharomyces cerevisiae, and Pyrococcus furiosus Rad50/Mre11, Escherichia coli SbcCD, and S.cerevisiae SMC1/SMC3 cohesin SMC complexes. Two distinct architectural arrangements are described, based on the way their components were connected. The eukaryotic complexes were similar to each other and differed from their prokaryotic and archaeal homologs. These similarities and differences are discussed with respect to their diverse mechanistic roles in chromosome metabolism.

AB - Structural maintenance of chromosomes (SMC) proteins have diverse cellular functions including chromosome segregation, condensation and DNA repair. They are grouped based on a conserved set of distinct structural motifs. All SMC proteins are predicted to have a bipartite ATPase domain that is separated by a long region predicted to form a coiled coil. Recent structural data on a variety of SMC proteins shows them to be arranged as long intramolecular coiled coils with a globular ATPase at one end. SMC proteins function in pairs as heterodimers or as homodimers often in complexes with other proteins. We expect the arrangement of the SMC protein domains in complex assemblies to have important implications for their diverse functions. We used scanning force microscopy imaging to determine the architecture of human, Saccharomyces cerevisiae, and Pyrococcus furiosus Rad50/Mre11, Escherichia coli SbcCD, and S.cerevisiae SMC1/SMC3 cohesin SMC complexes. Two distinct architectural arrangements are described, based on the way their components were connected. The eukaryotic complexes were similar to each other and differed from their prokaryotic and archaeal homologs. These similarities and differences are discussed with respect to their diverse mechanistic roles in chromosome metabolism.

KW - DNA metabolism

KW - SFM, scanning force microscopy

KW - SMC, structural maintenance of chromosomes

KW - SbcCD

KW - protein architecture

KW - scanning force microscopy (SFM)

KW - structural maintenance of chromosomes (SMC)

UR - http://www.scopus.com/inward/record.url?scp=2542427462&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2542427462&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2004.04.014

DO - 10.1016/j.jmb.2004.04.014

M3 - Article

C2 - 15165861

AN - SCOPUS:2542427462

VL - 339

SP - 937

EP - 949

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 4

ER -