Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis

Golldack D, Popova OV, Dietz K-J (2002)
JOURNAL OF BIOLOGICAL CHEMISTRY 277(7): 5541-5547.

Zeitschriftenaufsatz | Veröffentlicht| Englisch
 
Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Abstract / Bemerkung
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 on-set 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.
Erscheinungsjahr
2002
Zeitschriftentitel
JOURNAL OF BIOLOGICAL CHEMISTRY
Band
277
Ausgabe
7
Seite(n)
5541-5547
ISSN
0021-9258
eISSN
1083-351X
Page URI
https://pub.uni-bielefeld.de/record/1615275

Zitieren

Golldack D, Popova OV, Dietz K-J. Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis. JOURNAL OF BIOLOGICAL CHEMISTRY. 2002;277(7):5541-5547.
Golldack, D., Popova, O. V., & Dietz, K. - J. (2002). Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis. JOURNAL OF BIOLOGICAL CHEMISTRY, 277(7), 5541-5547. doi:10.1074/jbc.M106197200
Golldack, D., Popova, O. V., and Dietz, K. - J. (2002). Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis. JOURNAL OF BIOLOGICAL CHEMISTRY 277, 5541-5547.
Golldack, D., Popova, O.V., & Dietz, K.-J., 2002. Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis. JOURNAL OF BIOLOGICAL CHEMISTRY, 277(7), p 5541-5547.
D. Golldack, O.V. Popova, and K.-J. Dietz, “Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis”, JOURNAL OF BIOLOGICAL CHEMISTRY, vol. 277, 2002, pp. 5541-5547.
Golldack, D., Popova, O.V., Dietz, K.-J.: Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis. JOURNAL OF BIOLOGICAL CHEMISTRY. 277, 5541-5547 (2002).
Golldack, Dortje, Popova, OV, and Dietz, Karl-Josef. “Mutation of the matrix metalloproteinase At2-MMP inhibits growth and causes late flowering and early senescence in Arabidopsis”. JOURNAL OF BIOLOGICAL CHEMISTRY 277.7 (2002): 5541-5547.

42 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Genomewide association study of ionomic traits on diverse soybean populations from germplasm collections.
Ziegler G, Nelson R, Granada S, Krishnan HB, Gillman JD, Baxter I., Plant Direct 2(1), 2018
PMID: 31245681
SiYGL2 Is Involved in the Regulation of Leaf Senescence and Photosystem II Efficiency in Setaria italica (L.) P. Beauv.
Zhang S, Zhi H, Li W, Shan J, Tang C, Jia G, Tang S, Diao X., Front Plant Sci 9(), 2018
PMID: 30233633
Cell Death Control by Matrix Metalloproteinases.
Zimmermann D, Gomez-Barrera JA, Pasule C, Brack-Frick UB, Sieferer E, Nicholson TM, Pfannstiel J, Stintzi A, Schaller A., Plant Physiol 171(2), 2016
PMID: 27208293
SASP, a Senescence-Associated Subtilisin Protease, is involved in reproductive development and determination of silique number in Arabidopsis.
Martinez DE, Borniego ML, Battchikova N, Aro EM, Tyystjärvi E, Guiamét JJ., J Exp Bot 66(1), 2015
PMID: 25371504
Two homologous protein S-acyltransferases, PAT13 and PAT14, cooperatively regulate leaf senescence in Arabidopsis.
Lai J, Yu B, Cao Z, Chen Y, Wu Q, Huang J, Yang C., J Exp Bot 66(20), 2015
PMID: 26160582
A new polymorphism on chromosome 6 associated with bolting tendency in sugar beet.
Broccanello C, Stevanato P, Biscarini F, Cantu D, Saccomani M., BMC Genet 16(), 2015
PMID: 26643662
Response to long-term NaHCO3-derived alkalinity in model Lotus japonicus Ecotypes Gifu B-129 and Miyakojima MG-20: transcriptomic profiling and physiological characterization.
Babuin MF, Campestre MP, Rocco R, Bordenave CD, Escaray FJ, Antonelli C, Calzadilla P, Gárriz A, Serna E, Carrasco P, Ruiz OA, Menendez AB., PLoS One 9(5), 2014
PMID: 24835559
Labeling and enrichment of Arabidopsis thaliana matrix metalloproteases using an active-site directed, marimastat-based photoreactive probe.
Lenger J, Kaschani F, Lenz T, Dalhoff C, Villamor JG, Köster H, Sewald N, van der Hoorn RA., Bioorg Med Chem 20(2), 2012
PMID: 21775155
Matrix metalloproteinases in plants: a brief overview.
Marino G, Funk C., Physiol Plant 145(1), 2012
PMID: 22084906
Senescence-associated proteases in plants.
Roberts IN, Caputo C, Criado MV, Funk C., Physiol Plant 145(1), 2012
PMID: 22242903
Matrix metalloproteinases in plants: a brief overview
Marino G, Funk C., Physiol Plant 145(1), 2012
PMID: IND44654223
Senescence‐associated proteases in plants
Roberts IN, Caputo C, Criado MV, Funk C., Physiol Plant 145(1), 2012
PMID: IND44687065
The Arabidopsis aminopeptidase LAP2 regulates plant growth, leaf longevity and stress response.
Waditee-Sirisattha R, Shibato J, Rakwal R, Sirisattha S, Hattori A, Nakano T, Takabe T, Tsujimoto M., New Phytol 191(4), 2011
PMID: 21569035
Role of NADPH oxidase-2 in lipopolysaccharide-induced matrix metalloproteinase expression and cell migration.
Kim SY, Lee JG, Cho WS, Cho KH, Sakong J, Kim JR, Chin BR, Baek SH., Immunol Cell Biol 88(2), 2010
PMID: 19935767
A matrix metalloproteinase mediates airway remodeling in Drosophila.
Glasheen BM, Robbins RM, Piette C, Beitel GJ, Page-McCaw A., Dev Biol 344(2), 2010
PMID: 20513443
The Wnt/planar cell polarity protein-tyrosine kinase-7 (PTK7) is a highly efficient proteolytic target of membrane type-1 matrix metalloproteinase: implications in cancer and embryogenesis.
Golubkov VS, Chekanov AV, Cieplak P, Aleshin AE, Chernov AV, Zhu W, Radichev IA, Zhang D, Dong PD, Strongin AY., J Biol Chem 285(46), 2010
PMID: 20837484
A membrane-bound matrix-metalloproteinase from Nicotiana tabacum cv. BY-2 is induced by bacterial pathogens.
Schiermeyer A, Hartenstein H, Mandal MK, Otte B, Wahner V, Schillberg S., BMC Plant Biol 9(), 2009
PMID: 19563670
Plant proteases: from phenotypes to molecular mechanisms.
van der Hoorn RA., Annu Rev Plant Biol 59(), 2008
PMID: 18257708
Plant extracellular matrix metalloproteinases
Flinn BarryS., Funct Plant Biol 35(12), 2008
PMID: IND44138957
Identification of peptidases in Nicotiana tabacum leaf intercellular fluid.
Delannoy M, Alves G, Vertommen D, Ma J, Boutry M, Navarre C., Proteomics 8(11), 2008
PMID: 18446799
Transcript level regulation of the vacuolar H(+)-ATPase subunit isoforms VHA-a, VHA-E and VHA-G in Arabidopsis thaliana.
Hanitzsch M, Schnitzer D, Seidel T, Golldack D, Dietz KJ., Mol Membr Biol 24(5-6), 2007
PMID: 17710654
Mislocalization and unconventional functions of cellular MMPs in cancer.
Strongin AY., Cancer Metastasis Rev 25(1), 2006
PMID: 16680575
Salt-dependent regulation of chloride channel transcripts in rice
Diedhiou CJ, Golldack D., Plant Sci 170(4), 2006
PMID: IND43813823
Production of Desmodus rotundus salivary plasminogen activator alpha1 (DSPAalpha1) in tobacco is hampered by proteolysis.
Schiermeyer A, Schinkel H, Apel S, Fischer R, Schillberg S., Biotechnol Bioeng 89(7), 2005
PMID: 15685597

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 11726650
PubMed | Europe PMC

Suchen in

Google Scholar