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Abstract
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| Among the C1A cysteine proteases, the plant cathepsin F-like group has been poorly studied. This paper describes the molecular and functional characterization of the HvPap-1 cathepsin F-like protein from barley. This peptidase is N-glycosylated and has to be processed to become active, being its own propeptide an important modulator of the peptidase activity. The expression pattern of its mRNA and protein suggest that it is involved in different proteolytic processes in the barley plant. HvPap-1 peptidase has been purified in E. coli and the recombinant protein is able to degrade different substrates, including barley grain proteins (hordeins, albumins and globulins) stored in the barley endosperm. It has been localised in protein bodies and vesicles of the embryo and it is induced in aleurones by GA treatment. These three features support the HvPap-1 implication in the storage protein mobilization during grain germination. In addition, a complex regulation exerted by the barley cystatins, which are cysteine protease inhibitors and by its own propeptide, is also described | |
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International
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Si |
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JCR
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Si |
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Title
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Journal of Experimental Botany |
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ISBN
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0022-0957 |
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Impact factor JCR
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4,818 |
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Impact info
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Datos JCR del año 2010 |
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Volume
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63 |
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10.1093/jxb/err313 |
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Journal number
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63 |
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From page
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4615 |
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To page
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4629 |
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Month
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SIN MES |
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Ranking
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