Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-6-13
pubmed:abstractText
Higher plant phosphoenolpyruvate carboxylase (PEPC) is subject to in vivo phosphorylation of a regulatory serine located in the N-terminal domain of the protein. Studies using synthetic peptide substrates and mutated phosphorylation domain photosynthetic PEPC (C4 PEPC) suggested that the interaction of phosphoenolpyruvate carboxylase kinase (PEPCk) with its target was not restricted to this domain. However, no further information was available as to where PEPCk-C4 PEPC interactions take place. In this work, we have studied the possible interaction of the conserved 19-amino acid C-terminal sequence of sorghum (Sorghum vulgare Pers cv Tamaran) C4 PEPC with PEPCk. In reconstituted assays, a C-terminal synthetic peptide containing this sequence (peptide C19) was found to inhibit the phosphorylation reaction by the partially purified Ca2+-independent PEPCk (50% inhibition of initial activity = 230 microm). This effect was highly specific because peptide C19 did not alter C4 PEPC phosphorylation by either a partially purified sorghum leaf Ca2+-dependent protein kinase or the catalytic subunit of mammalian protein kinase A. In addition, the Ca2+-independent PEPCk was partially but significantly retained in affinity chromatography using a peptide C19 agarose column. Because peptide C15 (peptide C19 lacking the last four amino acids, QNTG) also inhibited C4 PEPC phosphorylation, it was concluded that the amino acid sequence downstream from the QNTG motif was responsible for the inhibitory effect. Specific antibodies raised against peptide C19 revealed that native C4 PEPC could be in two different conformational states. The results are discussed in relation with the reported crystal structure of the bacterial (Escherichia coli) and plant (maize [Zea mays]) enzymes.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-10525297, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-10571893, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-10972876, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-11469590, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-11607171, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-11773521, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-12467579, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-1311681, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-1512216, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-16668168, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-2148159, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-2493217, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-6396163, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-7986087, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-8274031, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-8346924, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-9419230, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-942051, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-9630496, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-9871363, http://linkedlifedata.com/resource/pubmed/commentcorrection/12805637-9927652
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
132
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1097-106
pubmed:dateRevised
2010-9-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
A conserved 19-amino acid synthetic peptide from the carboxy terminus of phosphoenolpyruvate carboxylase inhibits the in vitro phosphorylation of the enzyme by the calcium-independent phosphoenolpyruvate carboxylase kinase.
pubmed:affiliation
Departamento de Biología Vegetal, Facultad de Biología, Universidad de Sevilla, Avenida Reina Mercedes Number 6, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't