Linked Life Data

19759340

Source:http://linkedlifedata.com/resource/pubmed/id/19759340

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2009-11-5
pubmed:abstractText
Plant cystatins are inhibitors of cysteine-proteases of the papain C1A and legumain C13 families. Cystatin data from multiple plant species have suggested that these inhibitors act as defense proteins against pests and pathogens and as regulators of protein turnover. In this study, we characterize the entire cystatin gene family from barley (Hordeum vulgare), which contain 13 nonredundant genes, and identify and characterize their target enzymes, the barley cathepsin L-like proteases. Cystatins and proteases were expressed and purified from Escherichia coli cultures. Each cystatin was found to have different inhibitory capability against barley cysteine-proteases in in vitro inhibitory assays using specific substrates. Real-time reverse transcription-polymerase chain reaction revealed that inhibitors and enzymes present a wide variation in their messenger RNA expression patterns. Their transcripts were mainly detected in developing and germinating seeds, and some of them were also expressed in leaves and roots. Subcellular localization of cystatins and cathepsin L-like proteases fused to green fluorescent protein demonstrated the presence of both protein families throughout the endoplasmic reticulum and the Golgi complex. Proteases and cystatins not only colocalized but also interacted in vivo in the plant cell, as revealed by bimolecular fluorescence complementation. The functional relationship between cystatins and cathepsin L-like proteases was inferred from their common implication as counterparts of mobilization of storage proteins upon barley seed germination. The opposite pattern of transcription expression in gibberellin-treated aleurones presented by inhibitors and enzymes allowed proteases to specifically degrade B, C, and D hordeins stored in the endosperm of barley seeds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1532-2548
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
151
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1531-45
pubmed:dateRevised
2010-11-2
pubmed:meshHeading
pubmed-meshheading:19759340-Cathepsin L, pubmed-meshheading:19759340-Cystatins, pubmed-meshheading:19759340-Cysteine Proteinase Inhibitors, pubmed-meshheading:19759340-DNA, Plant, pubmed-meshheading:19759340-Endoplasmic Reticulum, pubmed-meshheading:19759340-Gene Expression Regulation, Plant, pubmed-meshheading:19759340-Genes, Plant, pubmed-meshheading:19759340-Germination, pubmed-meshheading:19759340-Glutens, pubmed-meshheading:19759340-Golgi Apparatus, pubmed-meshheading:19759340-Hordeum, pubmed-meshheading:19759340-Multigene Family, pubmed-meshheading:19759340-Phylogeny, pubmed-meshheading:19759340-Plant Proteins, pubmed-meshheading:19759340-Recombinant Proteins, pubmed-meshheading:19759340-Seeds, pubmed-meshheading:19759340-Sequence Alignment, pubmed-meshheading:19759340-Sequence Analysis, DNA
pubmed:year
2009
pubmed:articleTitle
Characterization of the entire cystatin gene family in barley and their target cathepsin L-like cysteine-proteases, partners in the hordein mobilization during seed germination.
pubmed:affiliation
Centro de Biotecnología y Genómica de Plantas, Universidad Politécnica de Madrid, Campus Montegancedo Universidad Politécnica de Madrid, 28223-Pozuelo de Alarcón, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't