Breaking the singleton of germination protease

Jimin Pei, Nick V. Grishin

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

Germination protease (GPR) plays an important role in the germination of spores of Bacillus and Clostridium species. A few very similar GPRs form a singleton group without significant sequence similarities to any other proteins. Their active site locations and catalytic mechanisms are unclear, despite the recent 3-D structure determination of Bacillus megaterium GPR. Using structural comparison and sequence analysis, we show that GPR is homologous to bacterial hydrogenase maturation protease (HybD). HybD's activity relies on the recognition and binding of metal ions in Ni-Fe hydrogenase, its substrate. Two highly conserved motifs are shared among GPRs, hydrogenase maturation proteases, and another group of hypothetical proteins. Conservation of two acidic residues in all these homologs indicates that metal binding is important for their function. Our analysis helps localize the active site of GPRs and provides insight into the catalytic mechanisms of a superfamily of putative metal-regulated proteases.

Original languageEnglish (US)
Pages (from-to)691-697
Number of pages7
JournalProtein Science
Volume11
Issue number3
DOIs
StatePublished - 2002

Fingerprint

Germination
Peptide Hydrolases
Ground penetrating radar systems
Hydrogenase
Metals
Bacilli
Catalytic Domain
Bacillus megaterium
Clostridium
Spores
Bacillus
Sequence Analysis
Proteins
Metal ions
Ions
Conservation
Substrates

Keywords

  • Catalytic mechanism
  • Homology
  • Metalloprotease
  • Sequence motif
  • Structural comparison

ASJC Scopus subject areas

  • Biochemistry

Cite this

Breaking the singleton of germination protease. / Pei, Jimin; Grishin, Nick V.

In: Protein Science, Vol. 11, No. 3, 2002, p. 691-697.

Research output: Contribution to journalArticle

Pei, Jimin ; Grishin, Nick V. / Breaking the singleton of germination protease. In: Protein Science. 2002 ; Vol. 11, No. 3. pp. 691-697.
@article{3b3f66f08ef04fd18caa39adbe179704,
title = "Breaking the singleton of germination protease",
abstract = "Germination protease (GPR) plays an important role in the germination of spores of Bacillus and Clostridium species. A few very similar GPRs form a singleton group without significant sequence similarities to any other proteins. Their active site locations and catalytic mechanisms are unclear, despite the recent 3-D structure determination of Bacillus megaterium GPR. Using structural comparison and sequence analysis, we show that GPR is homologous to bacterial hydrogenase maturation protease (HybD). HybD's activity relies on the recognition and binding of metal ions in Ni-Fe hydrogenase, its substrate. Two highly conserved motifs are shared among GPRs, hydrogenase maturation proteases, and another group of hypothetical proteins. Conservation of two acidic residues in all these homologs indicates that metal binding is important for their function. Our analysis helps localize the active site of GPRs and provides insight into the catalytic mechanisms of a superfamily of putative metal-regulated proteases.",
keywords = "Catalytic mechanism, Homology, Metalloprotease, Sequence motif, Structural comparison",
author = "Jimin Pei and Grishin, {Nick V.}",
year = "2002",
doi = "10.1110/ps.27302",
language = "English (US)",
volume = "11",
pages = "691--697",
journal = "Protein Science",
issn = "0961-8368",
publisher = "Cold Spring Harbor Laboratory Press",
number = "3",

}

TY - JOUR

T1 - Breaking the singleton of germination protease

AU - Pei, Jimin

AU - Grishin, Nick V.

PY - 2002

Y1 - 2002

N2 - Germination protease (GPR) plays an important role in the germination of spores of Bacillus and Clostridium species. A few very similar GPRs form a singleton group without significant sequence similarities to any other proteins. Their active site locations and catalytic mechanisms are unclear, despite the recent 3-D structure determination of Bacillus megaterium GPR. Using structural comparison and sequence analysis, we show that GPR is homologous to bacterial hydrogenase maturation protease (HybD). HybD's activity relies on the recognition and binding of metal ions in Ni-Fe hydrogenase, its substrate. Two highly conserved motifs are shared among GPRs, hydrogenase maturation proteases, and another group of hypothetical proteins. Conservation of two acidic residues in all these homologs indicates that metal binding is important for their function. Our analysis helps localize the active site of GPRs and provides insight into the catalytic mechanisms of a superfamily of putative metal-regulated proteases.

AB - Germination protease (GPR) plays an important role in the germination of spores of Bacillus and Clostridium species. A few very similar GPRs form a singleton group without significant sequence similarities to any other proteins. Their active site locations and catalytic mechanisms are unclear, despite the recent 3-D structure determination of Bacillus megaterium GPR. Using structural comparison and sequence analysis, we show that GPR is homologous to bacterial hydrogenase maturation protease (HybD). HybD's activity relies on the recognition and binding of metal ions in Ni-Fe hydrogenase, its substrate. Two highly conserved motifs are shared among GPRs, hydrogenase maturation proteases, and another group of hypothetical proteins. Conservation of two acidic residues in all these homologs indicates that metal binding is important for their function. Our analysis helps localize the active site of GPRs and provides insight into the catalytic mechanisms of a superfamily of putative metal-regulated proteases.

KW - Catalytic mechanism

KW - Homology

KW - Metalloprotease

KW - Sequence motif

KW - Structural comparison

UR - http://www.scopus.com/inward/record.url?scp=0036180681&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036180681&partnerID=8YFLogxK

U2 - 10.1110/ps.27302

DO - 10.1110/ps.27302

M3 - Article

VL - 11

SP - 691

EP - 697

JO - Protein Science

JF - Protein Science

SN - 0961-8368

IS - 3

ER -