Linked Life Data

15215503

Source:http://linkedlifedata.com/resource/pubmed/id/15215503

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-6-24
pubmed:databankReference
pubmed:abstractText
Calreticulin (CRT), a major Ca2+ -sequestering protein, has been implicated in a variety of cellular functions such as Ca2+ storage, signaling and chaperone activity within the cytoplasm and endoplasmic reticulum. To investigate the biological role of CRT in rice, 21 partial cDNAs, encoding proteins that interacted with rice CRT in a yeast two-hybrid interaction-cloning system, were characterized and the nucleotide sequences were found to be identical to each other. A full-length cDNA of 3.5 kb, obtained from rice genomic sequence data and 5' RACE, codes for a novel protein of 966 amino acid residues and was designated as CRTintP (CRT interacting protein). Primary sequence analysis of CRTintP showed no sequence homology with the known functional proteins; however, a potential ubiquitin-like domain at the N-terminal together with a putative leucine zipper, a nuclear localization signal and several sites for serine/threonine kinases were evident. Cellular localization of CRTintP demonstrated its role in directing green fluorescent protein to the nucleus in onion epidermal cells. Northern and immunoblot analysis showed increased expression of CRT and CRTintP in response to cold stress. Co-immunoprecipitation using anti-CRT antibodies confirmed the existence of the CRT-CRTintP complex in vivo in the stressed leaf tissue, suggesting their potential role in regulating stress response.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0032-0781
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
684-92
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15215503-Active Transport, Cell Nucleus, pubmed-meshheading:15215503-Amino Acid Sequence, pubmed-meshheading:15215503-Base Sequence, pubmed-meshheading:15215503-Binding Sites, pubmed-meshheading:15215503-Calreticulin, pubmed-meshheading:15215503-Cell Nucleus, pubmed-meshheading:15215503-Cold Temperature, pubmed-meshheading:15215503-DNA, Complementary, pubmed-meshheading:15215503-Gene Expression Regulation, Plant, pubmed-meshheading:15215503-Green Fluorescent Proteins, pubmed-meshheading:15215503-Luminescent Proteins, pubmed-meshheading:15215503-Molecular Sequence Data, pubmed-meshheading:15215503-Oryza sativa, pubmed-meshheading:15215503-Plant Epidermis, pubmed-meshheading:15215503-Plant Proteins, pubmed-meshheading:15215503-Protein Structure, Tertiary, pubmed-meshheading:15215503-Ubiquitins
pubmed:year
2004
pubmed:articleTitle
A novel interaction between calreticulin and ubiquitin-like nuclear protein in rice.
pubmed:affiliation
Japan Society for the Promotion of Science, Tsukuba, Ibaraki, 305-8602 Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't