Characterization of two novel subtilases from common bean (Phaseolus vulgaris L.) and their responses to drought

Plant Physiology and Biochemistry

Volumn 62, Issue , 2013, Pages 79-87

  Budič, MaruŠka ^a   Sabotič, Jerica ^a   Meglič, Vladimir ^c   Kos, Janko ^a,b   Kidrič, Marjetka ^a  

^a JO EF STEFAN INSTITUTE   (Slovenia)

^b UNIVERSITY OF LJUBLJANA   (Slovenia)

^c AGRICULTURAL INSTITUTE OF SLOVENIA   (Slovenia)

Author keywords

Common bean; Drought; Expression; Phaseolus vulgaris; Protease; Regulation; Subtilase

Indexed keywords

SUBTILASE, PLANT; SUBTILISIN;

AMINO ACID SEQUENCE; ARTICLE; BIOSYNTHESIS; ENZYMOLOGY; GENE EXPRESSION REGULATION; GENETICS; MOLECULAR GENETICS; PHASEOLUS; PHYSIOLOGICAL STRESS; PHYSIOLOGY; PLANT LEAF;

AMINO ACID SEQUENCE; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENE EXPRESSION REGULATION, PLANT; MOLECULAR SEQUENCE DATA; PHASEOLUS; PLANT LEAVES; STRESS, PHYSIOLOGICAL; SUBTILISINS;

ARACHIS HYPOGAEA; PHASEOLUS VULGARIS;

EID: 84870361173     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2012.10.022     Document Type: Article

References (44)

1. Schaller A. A cut above the rest: the regulatory function of plant proteases. Planta 2004, 220:183-197.
2. Antão C.M., Malcata F.X. Plant serine proteases: biochemical, physiological and molecular features. Plant Physiol. Biochem. 2005, 43:637-650.
3. Rawlings N.D., Barrett A.J., Bateman A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 2012, 40:D343-D350.
4. Schaller A., Stintzi A., Graff L. Subtilases - versatile tools for protein turnover, plant development, and interactions with the environment. Physiol. Plant 2012, 145:52-66.
5. Dodson G., Wlodawer A. Catalytic triads and their relatives. Trends Biochem. Sci. 1998, 23:347-352.
6. Rautengarten C., Steinhauser D., Büssis D., Stintzi A., Schaller A., Kopka J., Altmann T. Inferring hypotheses on functional relationships of genes: analysis of the Arabidopsis thaliana subtilase gene family. PLoS Comput. Biol. 2005, 1:e40.
7. Tripathi L., Sowdhamini R. Cross genome comparisons of serine proteases in Arabidopsis and rice. BMC Genomics 2006, 7:200.
8. Meichtry J., Amrhein N., Schaller A. Characterization of the subtilase gene family in tomato (Lycopersicon esculentum Mill.). Plant Mol. Biol. 1999, 39:749-760.
9. Barnaby N.G., He F., Liu X., Wilson K.A., Wilson K.A., Tan-Wilson A. Light-responsive subtilisin-related protease in soybean seedling leaves. Plant Physiol. Biochem. 2004, 42:125-134.
10. Popovič T., Puizdar V., Brzin J. A novel subtilase from common bean leaves. FEBS Lett. 2002, 530:163-168.
11. Vierstra R.D. Proteolysis in plants: mechanisms and functions. Plant Mol. Biol. 1996, 32:275-302.
12. Thompson A.R., Vierstra R.D. Autophagic recycling: lessons from yeast help define the process in plants. Curr. Opin. Plant Biol. 2005, 8:165-173.
13. Vaseva I., Sabotič J., Šustar-Vozlič J., Meglič V., Kidrič M., Demirevska K., Simova-Stoilova L. The response of plants to drought stress: the role of dehydrins, chaperones, proteases and protease inhibitors in maintaining cellular protein function. Droughts: New Research 2012, 1-45. Nova Science Publishers, Inc., New York. D.F. Neves, J.D. Sanz (Eds.).
14. Hauβühl K., Andersson B., Adamska I. A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II. EMBO J. 2001, 20:713-722.
15. Pinheiro C., Kehr J., Ricardo C.P. Effect of water stress on lupin stem protein analysed by two-dimensional gel electrophoresis. Planta 2005, 221:716-728.
16. Dramé K.N., Clavel D., Repellin A., Passaquet C., Zuily-Fodil Y. Water deficit induces variation in expression of stress-responsive genes in two peanut (Arachis hypogaea L.) cultivars with different tolerance to drought. Plant Physiol. Biochem. 2007, 45:236-243.
17. Hieng B., Ugrinović K., ŠuŠtar-Vozlič J., Kidrič M. Different classes of proteases are involved in the response to drought of Phaseolus vulgaris L. cultivars differing in sensitivity. J. Plant Physiol. 2004, 161:519-530.
18. Budič M., Kidrič M., Meglič V., Cigić B. A quantitative technique for determining proteases and their substrate specificities and pH optima in crude enzyme extracts. Anal. Biochem. 2009, 388:56-62.
19. 2+-independence and activation by homodimerization of tomato subtilase 3. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:17223-17228.
20. Yamagata H., Uesugi M., Saka K., Iwasaki T., Aizono Y. Molecular cloning and characterization of a cDNA and a gene for subtilisin-like serine proteases from rice (Oryza sativa L.) and Arabidopsis thaliana. Biosci. Biotechnol. Biochem. 2000, 64:1947-1957.
21. Roberts I., Passeron S., Barneix A. The two main endoproteases present in dark-induced senescent wheat leaves are distinct subtilisin-like proteases. Planta 2006, 224:1437-1447.
22. Bray E.A. Plant responses to water deficit. Trends Plant Sci. 1997, 2:48-54.
23. Floris M., Mahgoub H., Lanet E., Robaglia C., Menand B. Post-transcriptional regulation of gene expression in plants during abiotic stress. Int. J. Mol. Sci. 2009, 10:3168-3185.
24. Mazzucotelli E., Mastrangelo A.M., Crosatti C., Guerra D., Stanca A.M., Cattivelli L. Abiotic stress response in plants: when post-transcriptional and post-translational regulations control transcription. Plant Sci. 2008, 174:420-431.
25. Contour-Ansel D., Torres-Franklin M.L., Zuily-Fodil Y., de Carvalho M.H.C. An aspartic acid protease from common bean is expressed 'on call' during water stress and early recovery. J. Plant Physiol. 2010, 167:1606-1612.
26. Cruz de Carvalho M.H., d'Arcy-Lameta A., Roy-Macauley H., Gareil M., El Maarouf H., Pham-Thi A.-T., Zuily-Fodil Y. Aspartic protease in leaves of common bean (Phaseolus vulgaris L.) and cowpea (Vigna unguiculata L. Walp): enzymatic activity, gene expression and relation to drought susceptibility. FEBS Lett. 2001, 492:242-246.
27. Degenkolbe T., Do P., Zuther E., Repsilber D., Walther D., Hincha D., Köhl K. Expression profiling of rice cultivars differing in their tolerance to long-term drought stress. Plant Mol. Biol. 2009, 69:133-153.
28. Simova-Stoilova L., Vaseva I., Grigorova B., Demirevska K., Feller U. Proteolytic activity and cysteine protease expression in wheat leaves under severe soil drought and recovery. Plant Physiol. Biochem. 2010, 48:200-206.
29. Jain M., Khurana P., Tyagi A., Khurana J. Genome-wide analysis of intronless genes in rice and Arabidopsis. Funct. Integr. Genomics 2008, 8:69-78.
30. Beers E.P., Jones A.M., Dickerman A.W. The S8 serine, C1A cysteine and A1 aspartic protease families in Arabidopsis. Phytochemistry 2004, 65:43-58.
31. García-Lorenzo M., Sjödin A., Jansson S., Funk C. Protease gene families in Populus and Arabidopsis. BMC Plant Biol. 2006, 6:30.
32. Jorda L., Coego A., Conejero V., Vera P. A genomic cluster containing four differentially regulated subtilisin-like processing protease genes is in tomato plants. J. Biol. Chem. 1999, 274:2360-2365.
33. Jordá L., Conejero V., Vera P. Characterization of P69E and P69F, two differentially regulated genes encoding new members of the subtilisin-like proteinase family from tomato plants. Plant Physiol. 2000, 122:67-74.
34. Janzik I., Macheroux P., Amrhein N., Schaller A. LeSBT1 a subtilase from tomato plants. Overexpression in insect cells, purification, and characterization. J. Biol. Chem. 2000, 275:5193-5199.
35. Coffeen W.C., Wolpert T.J. Purification and characterization of serine proteases that exhibit caspase-like activity and are associated with programmed cell death in Avena sativa. Plant Cell 2004, 16:857-873.
36. Munne-Bosch S., Alegre L. Die and let live: leaf senescence contributes to plant survival under drought stress. Funct. Plant Biol. 2004, 31:203-216.
37. Golldack D., Vera P., Dietz K.-J. Expression of subtilisin-like serine proteases in Arabidopsis thaliana is cell-specific and responds to jasmonic acid and heavy metals with developmental differences. Physiol. Plant 2003, 118:64-73.
38. Roy-Macauley H., Zuily-Fodil Y., Kidrič M., Pham Thi A.T., Vieira de Silva J. Effect of drought stress on proteolytic activities in Phaseolus and Vigna leaves from sensitive and resistant plants. Physiol. Plant 1992, 85:90-96.
39. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
40. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
41. Emanuelsson O., Nielsen H., Brunak S., von Heijne G. Predicting subcellular localization of proteins based on their N-terminal amino acid sequence. J. Mol. Biol. 2000, 300:1005-1016.
42. Bannai H., Tamada Y., Maruyama O., Nakai K., Miyano S. Extensive feature detection of N-terminal protein sorting signals. Bioinformatics 2002, 18:298-305.
43. Pompe-Novak M., Gruden K., Baebler Š., Krečič-Stres H., Kovač M., Jongsma M., Ravnikar M. Potato virus Y induced changes in the gene expression of potato (Solanum tuberosum L.). Physiol. Mol. Plant Pathol. 2005, 67:237-247.
44. Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 2001, 29:e45.