Characterization of two novel subtilases from common bean (Phaseolus vulgaris L.) and their responses to drought. 2013

Maruška Budič, and Jerica Sabotič, and Vladimir Meglič, and Janko Kos, and Marjetka Kidrič
Department of Biotechnology, Jožef Stefan Institute, Jamova cesta 39, SI1000 Ljubljana, Slovenia. maruska.budic@ijs.si

Protein breakdown by proteases is basic to the plant response to abiotic stresses such as drought. A large number of genes encoding proteases or putative proteases exist in plants. Only a few of those involved in the response to drought have been characterized, and their regulation is poorly understood. We have identified two new subtilases from leaves of Phaseolus vulgaris L. cultivar Zorin, PvSLP1 and PvSLP2. PvSLP1 was identified at the gene level, using primers based on the gene sequence of the putative drought induced serine protease from Arachis hypogaea L. In P. vulgaris, expression of the PvSLP1 transcript did not change on water withdrawal. PvSLP2 was isolated and characterized at the protein level, together with complete gene and cDNA sequences. The deduced amino acid sequences of both PvSLP1 and PvSLP2 are characteristic of plant subtilases of the S8 family of clan SB. PvSLP2 shows 33% sequence identity to PvSLP1. Expression of the PvSLP2 transcript did not change on withdrawal of water, but its proteolytic activity in leaves increased, depending on the age and position of the leaf. In addition, the level of activity in senescent leaves of well watered plants was higher than in mature or young leaves. These results, together with the fact that PvSLP2 cleaves peptide bonds following an Arg residue, point to regulation of PvSLP2 subtilase activity at translational and/or post-translational levels and suggest a specific role in the response to drought and senescence.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D013312 Stress, Physiological The unfavorable effect of environmental factors (stressors) on the physiological functions of an organism. Prolonged unresolved physiological stress can affect HOMEOSTASIS of the organism, and may lead to damaging or pathological conditions. Biotic Stress,Metabolic Stress,Physiological Stress,Abiotic Stress,Abiotic Stress Reaction,Abiotic Stress Response,Biological Stress,Metabolic Stress Response,Physiological Stress Reaction,Physiological Stress Reactivity,Physiological Stress Response,Abiotic Stress Reactions,Abiotic Stress Responses,Abiotic Stresses,Biological Stresses,Biotic Stresses,Metabolic Stress Responses,Metabolic Stresses,Physiological Stress Reactions,Physiological Stress Responses,Physiological Stresses,Reaction, Abiotic Stress,Reactions, Abiotic Stress,Response, Abiotic Stress,Response, Metabolic Stress,Stress Reaction, Physiological,Stress Response, Metabolic,Stress Response, Physiological,Stress, Abiotic,Stress, Biological,Stress, Biotic,Stress, Metabolic
D013381 Subtilisins A family of SERINE ENDOPEPTIDASES isolated from Bacillus subtilis. EC 3.4.21.- Alcalase,AprA-Subtilisin,Bacillus amyloliquefaciens Serine Protease,Bacillus subtilis Alkaline Proteinase,Carlsberg Subtilisin,Maxatase,Nagarse,Novo Alcalase,Profezim,Protease VII,Subtilisin 72,Subtilisin A,Subtilisin BPN',Subtilisin Carlsberg,Subtilisin DY,Subtilisin E,Subtilisin GX,Subtilisin Novo,Subtilopeptidase A,Alcalase, Novo,AprA Subtilisin,Subtilisin, Carlsberg
D015971 Gene Expression Regulation, Enzymologic Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis. Enzymologic Gene Expression Regulation,Regulation of Gene Expression, Enzymologic,Regulation, Gene Expression, Enzymologic
D018506 Gene Expression Regulation, Plant Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants. Plant Gene Expression Regulation,Regulation of Gene Expression, Plant,Regulation, Gene Expression, Plant
D018515 Plant Leaves Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed) Plant Leaf,Leaf, Plant,Leave, Plant,Leaves, Plant,Plant Leave
D027805 Phaseolus A plant genus in the family FABACEAE which is the source of edible beans and the lectin PHYTOHEMAGGLUTININS. Bean, Kidney,Bean, Tepary,Kidney Bean,Tepary Bean,Common Bean Plant,French Bean Plant,Phaseolus acutifolius,Phaseolus vulgaris,Bean Plant, Common,Bean Plant, French,Bean Plants, Common,Bean Plants, French,Beans, Kidney,Beans, Tepary,Common Bean Plants,French Bean Plants,Kidney Beans,Phaseolus vulgari,Plant, Common Bean,Plant, French Bean,Plants, Common Bean,Plants, French Bean,Tepary Beans,vulgaris, Phaseolus

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