Genomic Clone

2011 ◽  
Keyword(s):  
Genomic Clone

scholarly journals Isolation of a genomic clone for Drosophila sn-glycerol-3-phosphate dehydrogenase using synthetic oligonucleotides.

1986 ◽  
Vol 261 (25) ◽  
pp. 11751-11755
Author(s):  
J L Cook ◽  
J B Shaffer ◽  
G C Bewley ◽  
R J MacIntyre ◽  
D A Wright
Keyword(s):  
Genomic Clone ◽  
Glycerol 3 Phosphate Dehydrogenase ◽  
Synthetic Oligonucleotides

scholarly journals Chicken calmodulin genes. A species comparison of cDNA sequences and isolation of a genomic clone.

1983 ◽  
Vol 258 (19) ◽  
pp. 11864-11870 ◽  
Author(s):  
J A Putkey ◽  
K F Ts'ui ◽  
T Tanaka ◽  
L Lagacé ◽  
J P Stein ◽  
...  
Keyword(s):  
Genomic Clone ◽  
Species Comparison ◽  
Cdna Sequences

scholarly journals An extracellular matrix protein in plants: characterization of a genomic clone for carrot extensin

1985 ◽  
Vol 4 (9) ◽  
pp. 2145-2151 ◽  
Author(s):  
Jychian Chen ◽  
Joseph E. Varner
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Genomic Clone ◽  
Extracellular Matrix Protein

Molecular analysis of an alcohol dehydrogenase-encoding genomic clone (adh2) from rice

Gene ◽  
1990 ◽  
Vol 87 (2) ◽  
pp. 185-191 ◽  
Author(s):  
Yong Xie ◽  
Ray Wu
Keyword(s):  
Alcohol Dehydrogenase ◽  
Molecular Analysis ◽  
Genomic Clone

scholarly journals Construction of the full coding information for murine J-chain protein from cDNA and its homologous genomic clone

1987 ◽  
Vol 15 (4) ◽  
pp. 1876-1876
Author(s):  
Rachel Gollop ◽  
Arieh Zaritsky
Keyword(s):  
Genomic Clone ◽  
J Chain

scholarly journals Detection of two chromatin proteins which bind specifically to the 5'-flanking region of the rat prolactin gene.

1985 ◽  
Vol 5 (11) ◽  
pp. 2967-2974 ◽  
Author(s):  
B A White ◽  
G M Preston ◽  
T C Lufkin ◽  
C Bancroft
Keyword(s):  
Transcription Initiation ◽  
Genomic Clone ◽  
Gh3 Cells ◽  
Pituitary Cells ◽  
Sequence Specificity ◽  
Strong Binding ◽  
Prolactin Gene ◽  
Rat Pituitary ◽  
Chromatin Proteins ◽  
Flanking Region

We employed a protein gel blotting procedure to search for nuclear proteins from rat pituitary cells that bind preferentially to the 5'-flanking region of the rat prolactin gene. By gel blots of chromatin proteins from GH3 rat pituitary tumor cells with a 32P-labeled prolactin genomic clone, we detected two major binding proteins with molecular weights of approximately 44,000 and 48,000, designated NP44 and NP48, respectively. Both NP44 and NP48 are minor chromatin proteins which are extracted at low salt concentrations (0.4 M NaCl) and exhibit a range of slightly acidic isoelectric variants. NP44 and NP48 were detected at similar levels in chromatin extracts of GH3 cells, the prolactin-negative GC cell variant of the GH3 cells, and normal rat pituitary tissue. Considerably lower levels of these two proteins were found in chromatin extracts from rat liver and rat C6 glial cells. NP44 and NP48 exhibit DNA sequence specificity, as evidenced by their strong binding to the upstream flanking region of the prolactin gene, but only very weak binding to plasmid DNA, rat prolactin or growth hormone cDNAs, or upstream flanking regions of two other rat genes. By analyzing subclones of a rat prolactin genomic clone, we established that NP44 and NP48 bind to at least two sites, which are located between 0.4 and 2.0 kilobases (region I) and between 2.0 and 4.8 kilobases (region II) upstream of the transcription initiation site. These findings are discussed in the context of a possible functional association between the strong binding of NP44 and NP48 to the prolactin 5'-flanking region and pituitary-specific expression of the prolactin gene.

Expression of a gene for mouse eucaryotic elongation factor Tu during murine erythroleukemic cell differentiation

1987 ◽  
Vol 7 (11) ◽  
pp. 3929-3936
Author(s):  
W W Roth ◽  
P W Bragg ◽  
M V Corrias ◽  
N S Reddy ◽  
J N Dholakia ◽  
...  
Keyword(s):  
Steady State ◽  
Genomic Library ◽  
Elongation Factor ◽  
State Level ◽  
Genomic Clone ◽  
Elongation Factor Tu ◽  
Steady State Level ◽  
Similar Reduction ◽  
S1 Nuclease ◽  
Murine Erythroleukemia

The eucaryotic elongation factor Tu (eEF-Tu) is a single polypeptide with an approximate Mr of 53,000. During protein synthesis eEF-Tu promotes the binding of aminoacyl-tRNA to the ribosome. To study the expression of the gene(s) for this factor, a genomic clone was isolated that contains a mouse eEF-Tu gene. We screened a phage genomic library with a synthetic oligonucleotide probe complementary to a region of the Saccharomyces cerevisiae and Artemia sp. eEF-Tu genes which codes for an area that is highly conserved between both yeast and Artemia sp. eEF-Tu. From approximately 75,000 phage plaques we obtained five isolates with apparently identical inserts. All five clones contained a 3.8-kilobase EcoRI fragment that hybridized to additional oligonucleotide probes corresponding to different conserved regions of eEF-Tu. We sequenced the 5' end of one genomic clone and determined the length of the cloned fragment that was protected by eEF-Tu mRNA in S1 nuclease protection assays. A quantitative S1 nuclease protection assay was used to compare the relative steady-state levels of eEF-Tu mRNA in total mRNA in total RNA isolated from hexamethylene-bisacetamide-induced murine erythroleukemia cells. The results show a dramatic reduction in the steady-state level of eEF-Tu mRNA as differentiation proceeds. A similar reduction in transcription of eEF-Tu mRNA was observed in isolated nuclei. Finally, we examined the in vivo synthesis of eEF-Tu during differentiation and found that it declined in a manner parallel to the decline in the steady-state level of eEF-Tu mRNA. In addition, we have isolated and sequenced a cDNA clone for mouse eEF-Tu. The derived amino acid sequence is compared with sequences from other eucaryotes.

A genomic clone encoding a novel proliferation-dependent histone H2A.1 mRNA enriched in the poly(A)+ fraction

1990 ◽  
Vol 10 (6) ◽  
pp. 2848-2854
Author(s):  
L Fecker ◽  
P Ekblom ◽  
M Kurkinen ◽  
M Ekblom
Keyword(s):  
Genomic Sequence ◽  
Genomic Clone ◽  
Polyadenylation Signal ◽  
Histone H2a ◽  
Hairpin Loop ◽  
Coding Region ◽  
Genomic Clones ◽  
Histone Mrnas ◽  
Cellulose Column

Replication-dependent histone mRNAs are prime examples of nonpolyadenylated mRNAs. We isolated and characterized cDNAs and a genomic clone for a replication-dependent histone H2A.1 mRNA which segregated into the poly(A)+ fraction during mRNA isolation through an oligo(dT)-cellulose column. However, the results of sequencing of the genomic clone suggested that the mRNA did not contain a poly(A) tail. Instead, the genomic sequence revealed a nonterminal oligo(A) tract directly upstream from the typical 3'-terminal hairpin loop of replication-dependent histone mRNAs. The nonterminal oligo(A) tract consisted of 14 adenylate residues interrupted by one guanylate residue (A4GA10). We concluded that this short oligo(A) stretch mediated binding of the mRNA to oligo(dT) even after stringent washes with 0.1 M NaCl, indicating that rather short oligo(A) sequences can ensure binding to oligo(dT)-cellulose. The cDNA and genomic clones contained an AAATAAG sequence at the end of the coding region. It has been suggested that this sequence contains a polyadenylation signal in some yeast and mouse transcripts, but it does not function as a polyadenylation signal in the histone transcript described in this paper.

Characterization of a Mouse β1-Adrenergic Receptor Genomic Clone

1993 ◽  
Vol 12 (6) ◽  
pp. 537-547 ◽  
Author(s):  
JEFFREY A. COHEN ◽  
LEE A. BAGGOTT ◽  
CARMELO ROMANO ◽  
MOTOMI ARAI ◽  
TAMARA E. SOUTHERLING ◽  
...  
Keyword(s):  
Adrenergic Receptor ◽  
Genomic Clone
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