Linked Life Data

7890164

Source:http://linkedlifedata.com/resource/pubmed/id/7890164

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-4-20
pubmed:databankReference
pubmed:abstractText
A cDNA clone was isolated from a Xenopus laevis embryo library and sequenced. Primer extension experiments indicated the full-length nature of the insert and the encoded product was identified on a two dimensional gel as ribosomal protein (r-protein) L22. The 510-bp L22 cDNA sequence presents short untranslated regions and a 5'-end polypyrimidine tract found in all other vertebrate r-protein mRNA (rp mRNA) so far analyzed. Both the nucleotide (nt) and the deduced amino acid (aa) sequences have been compared with the homologous sequences from other species. The L22 nt sequence is about 70% similar to the mammalian L27a rp mRNA and about 60% homologous to the Drosophila, Tetrahymena and yeast corresponding mRNAs. The 148-aa sequence presents a higher conservation, being 90% similar to the mammalian sequence and more than 70% to the other species. Expression analysis showed that, both during X. laevis embryogenesis and in X. laevis cultured cells during growth-rate changes, L22 synthesis is translationally regulated. Therefore X. laevis L22 mRNA is a new example of the correlation between the polypyrimidine terminal tract and the translational regulation observed in other rp mRNAs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0378-1119
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
199-203
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7890164-Amino Acid Sequence, pubmed-meshheading:7890164-Animals, pubmed-meshheading:7890164-Base Sequence, pubmed-meshheading:7890164-Conserved Sequence, pubmed-meshheading:7890164-Drosophila Proteins, pubmed-meshheading:7890164-Gene Expression Regulation, Developmental, pubmed-meshheading:7890164-Molecular Sequence Data, pubmed-meshheading:7890164-Protein Biosynthesis, pubmed-meshheading:7890164-Pyrimidines, pubmed-meshheading:7890164-RNA Processing, Post-Transcriptional, pubmed-meshheading:7890164-RNA-Binding Proteins, pubmed-meshheading:7890164-Regulatory Sequences, Nucleic Acid, pubmed-meshheading:7890164-Ribosomal Proteins, pubmed-meshheading:7890164-Sequence Homology, Amino Acid, pubmed-meshheading:7890164-Sequence Homology, Nucleic Acid, pubmed-meshheading:7890164-Xenopus Proteins, pubmed-meshheading:7890164-Xenopus laevis
pubmed:year
1995
pubmed:articleTitle
Xenopus laevis ribosomal protein L22: full-length cDNA sequence and expression analysis.
pubmed:affiliation
Dipartimento di Biologia, Università di Roma, Tor Vergata, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't