Construction and characterization of the soybean leaf metalloproteinase cDNA<sup>1</sup>

Pak, Jhang Ho; Liu, Chuan Y; Huangpu, Jun; Graham, John S.

doi:10.1016/s0014-5793(97)00141-5

Cited by 58 publications

(49 citation statements)

References 27 publications

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“…Expression increased up to the age of 20 days and increased slightly thereafter. The enzyme was neither expressed in young leaves nor in other tissues both on the transcript and on the protein level in soybean (10). In cucumber, the matrix metalloproteinase Cs1-MMP was detected in leaves during senescence with chlorophyll degradation already occurring.…”

Section: Discussionmentioning

confidence: 93%

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Mutation of the Matrix Metalloproteinase At2-MMP Inhibits Growth and Causes Late Flowering and Early Senescence in Arabidopsis

Golldack

Popova

Dietz

2002

Journal of Biological Chemistry

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This study characterizes the expression and functional significance of the member of the matrix metalloproteinase (MMP) family At2-MMP from Arabidopsis. By transcript analysis, expression of At2-MMP was found in leaves and roots of juvenile Arabidopsis and leaves, roots, and inflorescences of mature flowering plants showing strong increase of transcript abundance with aging. Cell specificity of expression of At2-MMP was studied by in situ hybridizations in leaves and flowers of Arabidopsis. In leaves, the gene was expressed in the phloem, in developing xylem elements, epidermal cells, and neighboring mesophyll cell layers. In flowers, signals were localized in pistils, ovules, and receptacles. In an Arabidopsis mutant (at2-mmp-1) carrying a tDNA insertion in At2-MMP, neither germination nor development of plants was modified in comparison to the wild type in the juvenile rosette stage. Starting with the onset of shoots, growth of roots, leaves, and shoots was inhibited compared with the wild type, and the plants were characterized by late flowering. Besides the flowering, at2-mmp-1 plants showed fast degradation of chlorophyll in leaves and early senescence. These results demonstrate the involvement of At2-MMP in plant growth, morphogenesis, and development with particular relevance for flowering and senescence.The family of zinc-dependent endopeptidases that has been particularly characterized in vertebrates is divided into four subfamilies based on structural and functional characteristics: matrix metalloproteinases (matrixins), adamalysins, serralysins, and astacins. All members of these zinc metalloproteinases have a similar structure with the conserved consensus sequence HEXXHXXGXXH in their catalytic site and a conserved methionine residue that forms the "Met-turn" structure (1). Members of the subfamily of matrix metalloproteinases are gelatinases, collagenases, and stromelysins (2). Matrix metalloproteinases are synthesized as prepro-enzymes with a signaling peptide targeting the enzyme to the extracellular space. The pre-domain is followed by a pro-peptide with a conserved PRCG(V/N)PD motif that contains the so-called "cysteine switch." This Cys residue ligates the catalytic zinc thus maintaining the latency of the inactive pro-enzymes (3). In vitro, pro-matrix metalloproteinases can be activated proteolytically by proteinases as well as by mercurial compounds and reactive oxygen, for example, whereas in vivo activation by proteinases is most likely (3). The function of matrix metalloproteinases is the degradation and remodeling of the extracellular matrix (2). The enzymes play a role in development, embryogenesis, and organ morphogenesis but also in wound healing in vertebrates (4). They also participate in pathological processes such as cancer and arthritis (5). In vertebrates, the enzyme activity of matrix metalloproteinases is transcriptionally regulated as well by proteolytic activation of the mature enzyme from the inactive pro-enzyme and by co-secretion with endogenous inhibitors (4).In addition ...

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Section: Discussionmentioning

confidence: 93%

“…The first matrix metalloproteinase (MMP) 1 isolated from higher plants was SMEP1 from soybean (9) that was subsequently cloned (10). SMEP1 was shown to be expressed in adult leaves but could not be detected in other plant tissues or in young developing leaves (10).…”

mentioning

confidence: 99%

Mutation of the Matrix Metalloproteinase At2-MMP Inhibits Growth and Causes Late Flowering and Early Senescence in Arabidopsis

Golldack

Popova

Dietz

2002

Journal of Biological Chemistry

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“…These invertebrate MMPs include envelysin from sea urchin [51][52][53], a Drosophila MMP [54]; and at least three separate MMPs from Caenorhabditis elegans [55]. Additional putative MMPs have been reported in plants such as soybean (Glycine max) [56], Arabidopsis thaliana [57], [58], and green alga [gamete lytic enzyme] [59]. Recent identification of MMP in hydra therefore adds a n e w m e m b e r t o t h e M M P f a m i l y o f metalloendopeptidases [44].…”

Section: Matrix Metalloproteinase (Mmp) In Hydramentioning

confidence: 99%

Structure, expression, and developmental function of early divergent forms of metalloproteinases in Hydra

Sarras

Li²,

Leontovich

et al. 2002

Cell Res

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Metalloproteinases have a critical role in a broad spectrum of cellular processes ranging from the breakdown of extracellular matrix to the processing of signal transduction-related proteins. These hydrolytic functions underlie a variety of mechanisms related to developmental processes as well as disease states. Structural analysis of metalloproteinases from both invertebrate and vertebrate species indicates that these enzymes are highly conserved and arose early during metazoan evolution. In this regard, studies from various laboratories have reported that a number of classes of metalloproteinases are found in hydra, a member of Cnidaria, the second oldest of existing animal phyla. These studies demonstrate that the hydra genome contains at least three classes of metalloproteinases to include members of the 1) astacin class, 2) matrix metalloproteinase class, and 3) neprilysin class. Functional studies indicate that these metalloproteinases play diverse and important roles in hydra morphogenesis and cell differentiation as well as specialized functions in adult polyps. This article will review the structure, expression, and function of these metalloproteinases in hydra.

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“…Several matrixins have been isolated from plants, including soybean (Graham et al, 1991;Liu et al, 2001;McGeehan et al, 1992;Pak et al, 1997), Arabidopsis (Maidment et al, 1999;Golldack et al, 2002), cucumber (Delorme et al, 2000), alfalfa (Combier et al, 2007), Pinus taeda (Ratnaparkhe et al, 2009), and Nicotiana tabacum (Schiermeyer, 2009). Matrixins have zinc at their catalytic center and are sensitive to EDTA (McGeehan et al, 1992).…”

mentioning

confidence: 99%

NMMP1, a Matrix Metalloprotease in Nicotiana benthamiana Has a Role in Protection against Bacterial Infection

Kang¹,

Oh²,

Kim³

et al. 2010

The Plant Pathology Journal

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Plant matrix metalloproteases (MMPs) are a family of apoplastic metalloproteases closely related to human matrilysins. Up-regulation of Nicotiana benthamiana matrix metalloprotease 1 (NMMP1) expression by treatment with pathogens, ethephon and aging indicates that the gene is related to plant defense and the aging process through ethylene signaling. NMMP1 expression was higher than in normal growth leaves following infection with an incompatible pathogen Pseudomonas syringae pv. tomato T1 or a compatible pathogen P. syringae pv. tabaci and in aged leaves. Transient overexpression of NMMP1 in N. benthamiana leaves lowered the growth of P. syringae pv. tabaci. However, NMMP1-silenced leaves showed increased growth of P. syringae pv. tabaci. These data strongly suggest that NMMP1 in N. benthamiana is a defense related gene, which is positively regulated by ethylene.

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Construction and characterization of the soybean leaf metalloproteinase cDNA¹

Cited by 58 publications

References 27 publications

Mutation of the Matrix Metalloproteinase At2-MMP Inhibits Growth and Causes Late Flowering and Early Senescence in Arabidopsis

Mutation of the Matrix Metalloproteinase At2-MMP Inhibits Growth and Causes Late Flowering and Early Senescence in Arabidopsis

Structure, expression, and developmental function of early divergent forms of metalloproteinases in Hydra

NMMP1, a Matrix Metalloprotease in Nicotiana benthamiana Has a Role in Protection against Bacterial Infection

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Construction and characterization of the soybean leaf metalloproteinase cDNA1

Cited by 58 publications

References 27 publications

Mutation of the Matrix Metalloproteinase At2-MMP Inhibits Growth and Causes Late Flowering and Early Senescence in Arabidopsis

Mutation of the Matrix Metalloproteinase At2-MMP Inhibits Growth and Causes Late Flowering and Early Senescence in Arabidopsis

Structure, expression, and developmental function of early divergent forms of metalloproteinases in Hydra

NMMP1, a Matrix Metalloprotease in Nicotiana benthamiana Has a Role in Protection against Bacterial Infection

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Construction and characterization of the soybean leaf metalloproteinase cDNA¹