About: Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis

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About: Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis
Creator	Liu, Jian-Xiang Srivastava, Renu Howell, Stephen
topic	covid:aea331cddd5eef46512ecea34503ed02af95d23e#this
Source	PMC
abstract	Phytosulfokines (PSKs) are secreted, sulfated peptide hormones derived from larger prepropeptide precursors. Proteolytic processing of one of the precursors, AtPSK4, was demonstrated by cleavage of a preproAtPSK4–myc transgene product to AtPSK4–myc. Cleavage of proAtPSK4 was induced by placing root explants in tissue culture. The processing of proAtPSK4 was dependent on AtSBT1.1, a subtilisin-like serine protease, encoded by one of 56 subtilase genes in Arabidopsis. The gene encoding AtSBT1.1 was up-regulated following the transfer of root explants to tissue culture, suggesting that activation of the proteolytic machinery that cleaves proAtPSK4 is dependent on AtSBT1.1 expression. We also demonstrated that a fluorogenic peptide representing the putative subtilase recognition site in proAtPSK4 is cleaved in vitro by affinity-purified AtSBT1.1. An alanine scan through the recognition site peptide indicated that AtSBT1.1 is fairly specific for the AtPSK4 precursor. Thus, this peptide growth factor, which promotes callus formation in culture, is proteolytically cleaved from its precursor by a specific plant subtilase encoded by a gene that is up-regulated during the process of transfering root explants to tissue culture.
has issue date	2008-08-01(xsd:dateTime)
bibo:doi	10.1111/j.1365-313x.2008.03598.x
bibo:pmid	18643977
has license	cc-by
sha1sum (hex)	aea331cddd5eef46512ecea34503ed02af95d23e
schema:url	https://doi.org/10.1111/j.1365-313x.2008.03598.x
resource representing a document's title	Proteolytic processing of a precursor protein for a growth-promoting peptide by a subtilisin serine protease in Arabidopsis
has PubMed Central identifier	PMC2667306
has PubMed identifier	18643977
schema:publication	Plant J
resource representing a document's body	covid:aea331cddd5eef46512ecea34503ed02af95d23e#body_text
is http://vocab.deri.ie/void#inDataset of	https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/aea331cddd5eef46512ecea34503ed02af95d23e
is schema:about of	named entity 'MACHINERY' named entity 'DEPENDENT' named entity 'INDICATED' named entity 'EXPRESSION' named entity 'CLEAVES' named entity 'DEMONSTRATED' named entity 'RECOGNITION' named entity 'SERINE PROTEASE' named entity 'ENCODING' named entity 'SUBTILISIN' named entity 'PLACING' named entity 'DERIVED' named entity 'PLANT' named entity 'IN VITRO' named entity 'UP-REGULATED' named entity 'FOLLOWING' named entity 'PRECURSOR' named entity 'PROTEOLYTIC PROCESSING' named entity 'PROTEIN ' named entity 'GROWTH' named entity 'PROMOTING' named entity 'LARGER' named entity 'ONE OF' named entity 'PROTEOLYTIC PROCESSING' named entity 'CLEAVED' named entity 'SECRETED' named entity 'ATPSK4' named entity 'PRODUCT' named entity 'PRECURSORS' named entity 'SUBTILASE' named entity 'PROTEOLYTIC' named entity 'PEPTIDE HORMONES' named entity 'ALANINE' named entity 'SERINE PROTEASE' named entity 'PEPTIDE' named entity 'ARABIDOPSIS' named entity 'PRECURSOR PROTEIN' named entity 'TRANSFER' named entity 'SITE' named entity 'LIKE' named entity 'CLEAVAGE' named entity 'ATSBT1.1' named entity 'ITS' named entity 'ACTIVATION' named entity 'PROCESS' named entity 'PEPTIDE' named entity 'TRANSGENE' named entity 'ENCODED' named entity 'INDUCED' named entity 'SUBTILISIN' named entity 'PROCESSING' named entity 'PURIFIED' named entity 'GROWTH FACTOR' named entity 'SPECIFIC' named entity 'SCAN' named entity 'ROOT' named entity 'A GENE' named entity 'GENES' named entity 'CALLUS FORMATION' named entity 'GENE' named entity 'MYC' named entity 'CULTURE' named entity 'ARABIDOPSIS' named entity 'AFFINITY' named entity 'TISSUE CULTURE' covid:arg/aea331cddd5eef46512ecea34503ed02af95d23e named entity 'recognition site' named entity 'fluorogenic' named entity 'gene' named entity 'Proteolytic processing' named entity 'gene' named entity 'callus formation' named entity 'prepropeptide' named entity 'myc' named entity 'N-terminal' named entity 'kinetin' named entity 'gene'

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