Source:http://linkedlifedata.com/resource/pubmed/id/11762197
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions |
umls-concept:C0002518,
umls-concept:C0006556,
umls-concept:C0026584,
umls-concept:C0166968,
umls-concept:C0205197,
umls-concept:C0322838,
umls-concept:C0439097,
umls-concept:C1413193,
umls-concept:C1426689,
umls-concept:C1547348,
umls-concept:C1705241,
umls-concept:C1711351,
umls-concept:C2717814,
umls-concept:C2752078
|
pubmed:issue |
3
|
pubmed:dateCreated |
2001-12-13
|
pubmed:databankReference | |
pubmed:abstractText |
The chaperonin containing t-complex polypeptide 1 (CCT) assists in the ATP-dependent folding and assembly of newly translated actin and tubulin in the eukaryotic cytosol. CCT is composed of eight different subunits, each encoded by an independent gene. In this report, we used RT-PCR amplification and 5'- and 3'-rapid amplification of cDNA ends (RACE) to determine the complete cDNA sequence of the CCT delta subunit from Aedes triseriatus mosquitoes. The CCT delta cDNA is 1936 nucleotides in length and encodes a putative 533 amino acid protein with a calculated molecular mass of 57,179 daltons and pI of 7.15. Hydrophobic residues comprise 39.8% of the amino acid sequence and putative motifs for ATP-binding and ATPase-activity are present. The amino acid sequence displays strong sequence similarity to Drosophila melanogaster (92%), human (85%), puffer fish (84%) and mouse (84%) counterparts. CCT delta mRNA was detected in both biosynthetically active (embryonating) and dormant (diapausing) Ae. triseriatus embryos by RT-PCR analysis.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/CCT4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Chaperonin Containing TCP-1,
http://linkedlifedata.com/resource/pubmed/chemical/Chaperonins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Subunits,
http://linkedlifedata.com/resource/pubmed/chemical/Tcp1 protein, mouse
|
pubmed:status |
MEDLINE
|
pubmed:issn |
1042-5179
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
12
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
203-8
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:11762197-Aedes,
pubmed-meshheading:11762197-Amino Acid Sequence,
pubmed-meshheading:11762197-Animals,
pubmed-meshheading:11762197-Base Sequence,
pubmed-meshheading:11762197-Chaperonin Containing TCP-1,
pubmed-meshheading:11762197-Chaperonins,
pubmed-meshheading:11762197-DNA, Complementary,
pubmed-meshheading:11762197-Molecular Sequence Data,
pubmed-meshheading:11762197-Protein Subunits
|
pubmed:year |
2001
|
pubmed:articleTitle |
Complete cDNA and deduced amino acid sequence of the chaperonin containing T-complex polypeptide 1 (CCT) delta subunit from Aedes triseriatus mosquitoes.
|
pubmed:affiliation |
Arthropod-Borne and Infectious Diseases Laboratory, Department of Microbiology, Colorado State University, Fort Collins, Colorado 80523, USA. blitvich@cvmbs.colostate.edu
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|