Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2001-10-8
pubmed:abstractText
The neuronal ceroid lipofuscinoses (NCLs) are the most common neurodegenerative disorders of childhood. The CLN1, CLN2 and CLN3 genes are associated to the infantile, late infantile and juvenile forms of NCL, respectively. We have subcloned the cDNAs encoding CLN1, CLN2 and BTN1, the yeast homologue of human CLN3, into plasmid vectors to evaluate whether these proteins interact with other proteins co-expressed from either a cDNA library derived from human cerebellum or from yeast, respectively, using the two-hybrid system. We concluded that CLN1 most likely does not interact with any other proteins in vivo. Furthermore, it is unlikely that CLN2 interacts with other proteins in vivo, although this study utilized a cDNA encoding the CLN2 precursor and it is possible that interacting partners may be excluded by the nature of this protein structure. Finally, we conclude that proteins that interact with Btn1p and therefore CLN3 cannot be identified using the whole proteins in a two-hybrid system, due to the hydrophobic nature of this protein. By understanding the topology of CLN3, specific regions of CLN3 need to be tested by two-hybrid to identify any interacting partners.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Aminopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/CLN3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/CLN3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Cyclins, http://linkedlifedata.com/resource/pubmed/chemical/Dipeptidyl-Peptidases and..., http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/PPT1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Serine Proteases, http://linkedlifedata.com/resource/pubmed/chemical/YHC3 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/tripeptidyl-peptidase 1
pubmed:status
MEDLINE
pubmed:issn
1090-3798
pubmed:author
pubmed:issnType
Print
pubmed:volume
5 Suppl A
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:11589016-Aminopeptidases, pubmed-meshheading:11589016-Child, pubmed-meshheading:11589016-Cyclins, pubmed-meshheading:11589016-Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, pubmed-meshheading:11589016-Endopeptidases, pubmed-meshheading:11589016-Fungal Proteins, pubmed-meshheading:11589016-Gene Expression, pubmed-meshheading:11589016-Humans, pubmed-meshheading:11589016-Membrane Glycoproteins, pubmed-meshheading:11589016-Membrane Proteins, pubmed-meshheading:11589016-Molecular Chaperones, pubmed-meshheading:11589016-Nerve Degeneration, pubmed-meshheading:11589016-Neuronal Ceroid-Lipofuscinoses, pubmed-meshheading:11589016-Peptide Hydrolases, pubmed-meshheading:11589016-Saccharomyces cerevisiae, pubmed-meshheading:11589016-Saccharomyces cerevisiae Proteins, pubmed-meshheading:11589016-Serine Proteases, pubmed-meshheading:11589016-Two-Hybrid System Techniques
pubmed:year
2001
pubmed:articleTitle
Searching for interacting partners of CLN1, CLN2 and Btn1p with the two-hybrid system.
pubmed:affiliation
Center for Aging and Developmental Biology, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't