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• W1977390532 abstract "Five genes potentially encoding novel matrix metalloproteinases (MMPs) have been identified on the Arabidopsis thaliana data base. The predicted proteins have a similar domain structure to mammalian MMP-7, with a propeptide and catalytic domain but no C-terminal hemopexin-like domain. Four of the A. thaliana MMPs (At-MMPs) have a predicted C-terminal transmembrane domain. The At-MMPs are differentially expressed in flower, leaf, root, and stem tissues from 14-day-old plants. The cDNA for one of the At-MMPs (At1-MMP) was cloned and expressed in Escherichia coli. Following refolding and purification, the proenzyme At1-MMP was shown to undergo autolytic activation in the presence of an organomercurial with a concomitant decrease inM r. In contrast to this, trypsin-treatment led to the formation of an inactive product. The activated At1-MMP digested myelin basic protein, but was unable to digest gelatin or casein. Three peptide substrates for MMPs were also cleaved by At1-MMP. The enzyme activity of At1-MMP was inhibited by human tissue inhibitors of metalloproteinases 1 and 2 and the hydroxamate inhibitor BB-94. Five genes potentially encoding novel matrix metalloproteinases (MMPs) have been identified on the Arabidopsis thaliana data base. The predicted proteins have a similar domain structure to mammalian MMP-7, with a propeptide and catalytic domain but no C-terminal hemopexin-like domain. Four of the A. thaliana MMPs (At-MMPs) have a predicted C-terminal transmembrane domain. The At-MMPs are differentially expressed in flower, leaf, root, and stem tissues from 14-day-old plants. The cDNA for one of the At-MMPs (At1-MMP) was cloned and expressed in Escherichia coli. Following refolding and purification, the proenzyme At1-MMP was shown to undergo autolytic activation in the presence of an organomercurial with a concomitant decrease inM r. In contrast to this, trypsin-treatment led to the formation of an inactive product. The activated At1-MMP digested myelin basic protein, but was unable to digest gelatin or casein. Three peptide substrates for MMPs were also cleaved by At1-MMP. The enzyme activity of At1-MMP was inhibited by human tissue inhibitors of metalloproteinases 1 and 2 and the hydroxamate inhibitor BB-94. matrix metalloproteinase A. thaliana MMP tissue inhibitor of metalloproteinases 4-aminophenyl mercuric acetate myelin basic protein reverse transcription polymerase chain reaction polyacrylamide gel electrophoresis The matrix metalloproteinases (MMPs)1 are a family of at least 20 zinc-dependent endoproteinases in vertebrates, capable of degrading extracellular matrix substrates; they have been divided into subgroups according to their structure and function. The MMPs have a common domain structure with a signal peptide, a propeptide, a catalytic domain, a hinge region, and a C-terminal domain. The propeptide contains an invariant Cys residue that ligates the active site zinc ion to maintain latency; the catalytic domain contains an HEXGHXXGXXH zinc-binding sequence characteristic of the metzincin superfamily of proteinases, followed by an invariant Met that is involved in a structural feature called the “Met-turn.” In all family members except matrilysin (MMP-7) a hinge region links to a hemopexin-like C-terminal domain that is thought to be involved in substrate specificity and binding of inhibitors. Individual MMPs contain variations on this theme: MT-MMPs (MMPs 14–17) have a transmembrane domain and cytoplasmic tail at the C terminus and, in common with MMP-11, contain a potential furin-cleavage site within the propeptide; the gelatinases (MMP-2 and -9) have an insert of three fibronectin type II repeats in the catalytic domain; and MMP-9 has a collagen-like sequence at one end of the catalytic domain (1Clark I.M. Murphy G. Matrix Proteinases Seibel M.J. Robins S.P. Bilezikian J.P. Dyamics of Bone and Cartilage Metabolism. Academic Press, San Diego, CA1999: 137-150Google Scholar).Invertebrates have also been shown to possess proteinases homologous to MMPs; these include the envelysins, which are involved in the hatching process in sea urchins (2Nomura K. Shimizu T. Kinoh H. Sendai Y. Inomata M. Suzuki N. Biochemistry. 1997; 36: 7225-7238Crossref PubMed Scopus (36) Google Scholar). A report has described three sequences inCaenorhabditis elegans that appear to correspond to MMPs (3Wada K. Sato H. Kinoh H. Kajita M. Yamamoto H. Seiki M. Gene. 1998; 211: 57-62Crossref PubMed Scopus (60) Google Scholar). In 1991, soybean leaves were shown to contain a metalloproteinase, later shown to be homologous to MMPs. This enzyme was expressed only in adult leaves, and Southern blot analysis demonstrated a single copy gene; activity was demonstrated against a synthetic MMP substrate, and this activity was inhibited by mammalian TIMP-1 (4Graham J.S. Xiong J. Gillikin J.W. Plant Physiol. 1991; 97: 786-792Crossref PubMed Scopus (61) Google Scholar, 5McGeehan G. Burkhart W. Anderegg R. Becherer J.D. Gillikin J.W. Graham J.S. Plant Physiol. 1992; 99: 1179-1183Crossref PubMed Scopus (55) Google Scholar, 6Pak J-H. Liu C.Y. Huangpu J. Graham J.S. FEBS Lett. 1997; 404: 283-288Crossref PubMed Scopus (51) Google Scholar).The plant Arabidopsis thaliana is an important model species for the study of plant biology, with many of the tools and reagents in place to manipulate genes in vivo. The relatively small size of its genome has led to a project to sequence its five chromosomes; our study began with the discovery within this project that a sequence on chromosome 4 of the A. thaliana genome codes for a protein with homology to both the soybean MMP and the vertebrate MMP family (7Bevan M. Bancroft I. Bent E. Love K. Goodman H. Dean C. Bergkamp R. Dirkse W. VanStaveren M. Stiekema W. Drost L. Ridley P. Hudson S.A. Patel K. Murphy G. Piffanelli P. Wedler H. Wedler E. Wambutt R. Weitzenegger T. Pohl T.M. Terryn N. Gielen J. Villarroel R. DeClerck R. VanMontagu M. Lecharny A. Auborg S. Gy I. Kreis M. Lao N. Kavanagh T. Hempel S. Kotter P. Entian K.D. Rieger M. Schaeffer M. Funk B. MuellerAuer S. Silvey M. James R. Montfort A. Pons A. Puigdomenech P. Douka A. Voukelatou E. Milioni D. Hatzopoulos P. Piravandi E. Obermaier B. Hilbert H. Dusterhoft A. Moores T. Jones J.D.G. Eneva T. Palme K. Benes V. Rechman S. Ansorge W. Cooke R. Berger C. Delseny M. Voet M. Volckaert G. Mewes H.W. Klosterman S. Schueller C. Chalwatzis N. Nature. 1999; 391: 419-516Google Scholar). During our studies, four other sequences with homology to this first one have been identified on the data base; we have named these At1-MMP to At5-MMP in order of our discovery of them on the computer (see below). Here, we examined expression of At1- to At5-MMP in tissues from A. thaliana and then cloned and expressed At1-MMP in Escherichia coli and examined its ability to cleave both protein and synthetic substrates and to be inhibited by known MMP inhibitors. The matrix metalloproteinases (MMPs)1 are a family of at least 20 zinc-dependent endoproteinases in vertebrates, capable of degrading extracellular matrix substrates; they have been divided into subgroups according to their structure and function. The MMPs have a common domain structure with a signal peptide, a propeptide, a catalytic domain, a hinge region, and a C-terminal domain. The propeptide contains an invariant Cys residue that ligates the active site zinc ion to maintain latency; the catalytic domain contains an HEXGHXXGXXH zinc-binding sequence characteristic of the metzincin superfamily of proteinases, followed by an invariant Met that is involved in a structural feature called the “Met-turn.” In all family members except matrilysin (MMP-7) a hinge region links to a hemopexin-like C-terminal domain that is thought to be involved in substrate specificity and binding of inhibitors. Individual MMPs contain variations on this theme: MT-MMPs (MMPs 14–17) have a transmembrane domain and cytoplasmic tail at the C terminus and, in common with MMP-11, contain a potential furin-cleavage site within the propeptide; the gelatinases (MMP-2 and -9) have an insert of three fibronectin type II repeats in the catalytic domain; and MMP-9 has a collagen-like sequence at one end of the catalytic domain (1Clark I.M. Murphy G. Matrix Proteinases Seibel M.J. Robins S.P. Bilezikian J.P. Dyamics of Bone and Cartilage Metabolism. Academic Press, San Diego, CA1999: 137-150Google Scholar). Invertebrates have also been shown to possess proteinases homologous to MMPs; these include the envelysins, which are involved in the hatching process in sea urchins (2Nomura K. Shimizu T. Kinoh H. Sendai Y. Inomata M. Suzuki N. Biochemistry. 1997; 36: 7225-7238Crossref PubMed Scopus (36) Google Scholar). A report has described three sequences inCaenorhabditis elegans that appear to correspond to MMPs (3Wada K. Sato H. Kinoh H. Kajita M. Yamamoto H. Seiki M. Gene. 1998; 211: 57-62Crossref PubMed Scopus (60) Google Scholar). In 1991, soybean leaves were shown to contain a metalloproteinase, later shown to be homologous to MMPs. This enzyme was expressed only in adult leaves, and Southern blot analysis demonstrated a single copy gene; activity was demonstrated against a synthetic MMP substrate, and this activity was inhibited by mammalian TIMP-1 (4Graham J.S. Xiong J. Gillikin J.W. Plant Physiol. 1991; 97: 786-792Crossref PubMed Scopus (61) Google Scholar, 5McGeehan G. Burkhart W. Anderegg R. Becherer J.D. Gillikin J.W. Graham J.S. Plant Physiol. 1992; 99: 1179-1183Crossref PubMed Scopus (55) Google Scholar, 6Pak J-H. Liu C.Y. Huangpu J. Graham J.S. FEBS Lett. 1997; 404: 283-288Crossref PubMed Scopus (51) Google Scholar). The plant Arabidopsis thaliana is an important model species for the study of plant biology, with many of the tools and reagents in place to manipulate genes in vivo. The relatively small size of its genome has led to a project to sequence its five chromosomes; our study began with the discovery within this project that a sequence on chromosome 4 of the A. thaliana genome codes for a protein with homology to both the soybean MMP and the vertebrate MMP family (7Bevan M. Bancroft I. Bent E. Love K. Goodman H. Dean C. Bergkamp R. Dirkse W. VanStaveren M. Stiekema W. Drost L. Ridley P. Hudson S.A. Patel K. Murphy G. Piffanelli P. Wedler H. Wedler E. Wambutt R. Weitzenegger T. Pohl T.M. Terryn N. Gielen J. Villarroel R. DeClerck R. VanMontagu M. Lecharny A. Auborg S. Gy I. Kreis M. Lao N. Kavanagh T. Hempel S. Kotter P. Entian K.D. Rieger M. Schaeffer M. Funk B. MuellerAuer S. Silvey M. James R. Montfort A. Pons A. Puigdomenech P. Douka A. Voukelatou E. Milioni D. Hatzopoulos P. Piravandi E. Obermaier B. Hilbert H. Dusterhoft A. Moores T. Jones J.D.G. Eneva T. Palme K. Benes V. Rechman S. Ansorge W. Cooke R. Berger C. Delseny M. Voet M. Volckaert G. Mewes H.W. Klosterman S. Schueller C. Chalwatzis N. Nature. 1999; 391: 419-516Google Scholar). During our studies, four other sequences with homology to this first one have been identified on the data base; we have named these At1-MMP to At5-MMP in order of our discovery of them on the computer (see below). Here, we examined expression of At1- to At5-MMP in tissues from A. thaliana and then cloned and expressed At1-MMP in Escherichia coli and examined its ability to cleave both protein and synthetic substrates and to be inhibited by known MMP inhibitors. This work would not have been possible without help and advice from Greg Dean, Vera Knäuper, Augustin Amour, Mike Hutton, Marc Lafleur, Ann Merryweather, and Nicola Williamson. N-terminal sequencing was performed by Mike Naldrett at the John Innes Centre Protein Sequencing and Peptide Synthesis Unit. BB-94 was a kind gift from British Biotech Pharmaceuticals Ltd. (Oxford, United Kingdom)." @default.
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• W1977390532 title "Matrix Metalloproteinase Homologues from Arabidopsis thaliana" @default.
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