Archaeal RecA homologues: Different response to DNA-damaging agents in mesophilic and thermophilic Archaea

Claudia I. Reich, Leslie K. McNeil, Jennifer L. Brace, Jacqueline K. Brucker, Gary J. Olsen

Research output: Contribution to journalArticle

Abstract

Two archaeal proteins, RadA and RadB, share similarity with the RecA/Rad51 family of recombinases, with RadA being the functional homologue. We have studied and compared the RadA and RadB proteins of mesophilic and thermophilic Archaea. In growing cells, RadA levels are similar in mesophilic Methanococcus species and the hyperthermophile Methanococcus jannaschii. Treatment of cells with mutagenic agents (methylmethane sulfonate or UV light) increased the expression of RadA (as evidenced by higher levels of both mRNA and protein) in all organisms tested, but the increase was greater in the mesophiles than in the thermophiles M. jannaschii and Sulfolobus solfataricus. Recombinantly expressed RadA proteins from the mesophile M. voltae and the thermophile M. jannaschii were similar in their ATPase- and DNA-binding activities. All the data are consistent with proposals that RadA plays the same role as eukaryotic Rad51. Surprisingly, the data also suggested that the thermophiles do not need more RadA protein or activity than the mesophiles. On the other hand, RadB is not coregulated with RadA, and its role remains unclear. Neither RadA nor RadB from a mesophile or from a thermophile rescued the UV-sensitive phenotype of an Escherichia coli recA- host.

Original languageEnglish (US)
Pages (from-to)265-275
Number of pages11
JournalExtremophiles
Volume5
Issue number4
DOIs
StatePublished - Dec 1 2001

Fingerprint

Methanocaldococcus
Archaea
DNA
Rad51 Recombinase
Proteins
Methanococcus
Sulfolobus solfataricus
Methyl Methanesulfonate
Ultraviolet Rays
Adenosine Triphosphatases
Escherichia coli
Phenotype
Messenger RNA

Keywords

  • DNA repair
  • Gene regulation
  • Rad51
  • RadA
  • RadB

ASJC Scopus subject areas

  • Microbiology
  • Molecular Medicine

Cite this

Archaeal RecA homologues : Different response to DNA-damaging agents in mesophilic and thermophilic Archaea. / Reich, Claudia I.; McNeil, Leslie K.; Brace, Jennifer L.; Brucker, Jacqueline K.; Olsen, Gary J.

In: Extremophiles, Vol. 5, No. 4, 01.12.2001, p. 265-275.

Research output: Contribution to journalArticle

Reich, Claudia I. ; McNeil, Leslie K. ; Brace, Jennifer L. ; Brucker, Jacqueline K. ; Olsen, Gary J. / Archaeal RecA homologues : Different response to DNA-damaging agents in mesophilic and thermophilic Archaea. In: Extremophiles. 2001 ; Vol. 5, No. 4. pp. 265-275.
@article{ec708b8a90a24703ac8c6719215dab0d,
title = "Archaeal RecA homologues: Different response to DNA-damaging agents in mesophilic and thermophilic Archaea",
abstract = "Two archaeal proteins, RadA and RadB, share similarity with the RecA/Rad51 family of recombinases, with RadA being the functional homologue. We have studied and compared the RadA and RadB proteins of mesophilic and thermophilic Archaea. In growing cells, RadA levels are similar in mesophilic Methanococcus species and the hyperthermophile Methanococcus jannaschii. Treatment of cells with mutagenic agents (methylmethane sulfonate or UV light) increased the expression of RadA (as evidenced by higher levels of both mRNA and protein) in all organisms tested, but the increase was greater in the mesophiles than in the thermophiles M. jannaschii and Sulfolobus solfataricus. Recombinantly expressed RadA proteins from the mesophile M. voltae and the thermophile M. jannaschii were similar in their ATPase- and DNA-binding activities. All the data are consistent with proposals that RadA plays the same role as eukaryotic Rad51. Surprisingly, the data also suggested that the thermophiles do not need more RadA protein or activity than the mesophiles. On the other hand, RadB is not coregulated with RadA, and its role remains unclear. Neither RadA nor RadB from a mesophile or from a thermophile rescued the UV-sensitive phenotype of an Escherichia coli recA- host.",
keywords = "DNA repair, Gene regulation, Rad51, RadA, RadB",
author = "Reich, {Claudia I.} and McNeil, {Leslie K.} and Brace, {Jennifer L.} and Brucker, {Jacqueline K.} and Olsen, {Gary J.}",
year = "2001",
month = "12",
day = "1",
doi = "10.1007/s007920100197",
language = "English (US)",
volume = "5",
pages = "265--275",
journal = "Extremophiles : life under extreme conditions",
issn = "1431-0651",
publisher = "Springer Japan",
number = "4",

}

TY - JOUR

T1 - Archaeal RecA homologues

T2 - Different response to DNA-damaging agents in mesophilic and thermophilic Archaea

AU - Reich, Claudia I.

AU - McNeil, Leslie K.

AU - Brace, Jennifer L.

AU - Brucker, Jacqueline K.

AU - Olsen, Gary J.

PY - 2001/12/1

Y1 - 2001/12/1

N2 - Two archaeal proteins, RadA and RadB, share similarity with the RecA/Rad51 family of recombinases, with RadA being the functional homologue. We have studied and compared the RadA and RadB proteins of mesophilic and thermophilic Archaea. In growing cells, RadA levels are similar in mesophilic Methanococcus species and the hyperthermophile Methanococcus jannaschii. Treatment of cells with mutagenic agents (methylmethane sulfonate or UV light) increased the expression of RadA (as evidenced by higher levels of both mRNA and protein) in all organisms tested, but the increase was greater in the mesophiles than in the thermophiles M. jannaschii and Sulfolobus solfataricus. Recombinantly expressed RadA proteins from the mesophile M. voltae and the thermophile M. jannaschii were similar in their ATPase- and DNA-binding activities. All the data are consistent with proposals that RadA plays the same role as eukaryotic Rad51. Surprisingly, the data also suggested that the thermophiles do not need more RadA protein or activity than the mesophiles. On the other hand, RadB is not coregulated with RadA, and its role remains unclear. Neither RadA nor RadB from a mesophile or from a thermophile rescued the UV-sensitive phenotype of an Escherichia coli recA- host.

AB - Two archaeal proteins, RadA and RadB, share similarity with the RecA/Rad51 family of recombinases, with RadA being the functional homologue. We have studied and compared the RadA and RadB proteins of mesophilic and thermophilic Archaea. In growing cells, RadA levels are similar in mesophilic Methanococcus species and the hyperthermophile Methanococcus jannaschii. Treatment of cells with mutagenic agents (methylmethane sulfonate or UV light) increased the expression of RadA (as evidenced by higher levels of both mRNA and protein) in all organisms tested, but the increase was greater in the mesophiles than in the thermophiles M. jannaschii and Sulfolobus solfataricus. Recombinantly expressed RadA proteins from the mesophile M. voltae and the thermophile M. jannaschii were similar in their ATPase- and DNA-binding activities. All the data are consistent with proposals that RadA plays the same role as eukaryotic Rad51. Surprisingly, the data also suggested that the thermophiles do not need more RadA protein or activity than the mesophiles. On the other hand, RadB is not coregulated with RadA, and its role remains unclear. Neither RadA nor RadB from a mesophile or from a thermophile rescued the UV-sensitive phenotype of an Escherichia coli recA- host.

KW - DNA repair

KW - Gene regulation

KW - Rad51

KW - RadA

KW - RadB

UR - http://www.scopus.com/inward/record.url?scp=0035431205&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035431205&partnerID=8YFLogxK

U2 - 10.1007/s007920100197

DO - 10.1007/s007920100197

M3 - Article

C2 - 11523896

AN - SCOPUS:0035431205

VL - 5

SP - 265

EP - 275

JO - Extremophiles : life under extreme conditions

JF - Extremophiles : life under extreme conditions

SN - 1431-0651

IS - 4

ER -