scholarly journals Nucleotide Sequence of a Wheat Chloroplastic Phosphoglycerate Kinase Gene

1995 ◽  
Vol 107 (4) ◽  
pp. 1483-1484 ◽  
Author(s):  
P. G. Jones ◽  
C. A. Raines ◽  
J. C. Lloyd
Keyword(s):  
Nucleotide Sequence ◽  
Phosphoglycerate Kinase ◽  
Kinase Gene ◽  
Phosphoglycerate Kinase Gene

The testis-specific phosphoglycerate kinase gene pgk-2 is a recruited retroposon

1987 ◽  
Vol 7 (9) ◽  
pp. 3107-3112
Author(s):  
P H Boer ◽  
C N Adra ◽  
Y F Lau ◽  
M W McBurney
Keyword(s):  
Nucleotide Sequence ◽  
Gene Duplication ◽  
X Chromosome ◽  
Phosphoglycerate Kinase ◽  
Sperm Cells ◽  
Kinase Gene ◽  
Evolutionary Diversification ◽  
Key Enzyme ◽  
Phosphoglycerate Kinase Gene ◽  
Kinase A

In both humans and mice, two genes encode phosphoglycerate kinase, a key enzyme in the glycolytic pathway. The pgk-1 gene is expressed in all somatic cells, is located on the X chromosome, and contains 10 introns. The pgk-2 gene is expressed only in sperm cells, is located on an autosome, and has no introns. The nucleotide sequence of the pgk-2 gene suggests that it arose from pgk-1 more than 100 million years ago by RNA-mediated gene duplication. The pgk-2 gene may, then, be a transcribed retroposon. Thus, gene duplication by retroposition may have been used as a mechanism for evolutionary diversification.

scholarly journals The testis-specific phosphoglycerate kinase gene pgk-2 is a recruited retroposon.

1987 ◽  
Vol 7 (9) ◽  
pp. 3107-3112 ◽  
Author(s):  
P H Boer ◽  
C N Adra ◽  
Y F Lau ◽  
M W McBurney
Keyword(s):  
Nucleotide Sequence ◽  
Gene Duplication ◽  
X Chromosome ◽  
Phosphoglycerate Kinase ◽  
Sperm Cells ◽  
Kinase Gene ◽  
Evolutionary Diversification ◽  
Key Enzyme ◽  
Phosphoglycerate Kinase Gene ◽  
Kinase A

In both humans and mice, two genes encode phosphoglycerate kinase, a key enzyme in the glycolytic pathway. The pgk-1 gene is expressed in all somatic cells, is located on the X chromosome, and contains 10 introns. The pgk-2 gene is expressed only in sperm cells, is located on an autosome, and has no introns. The nucleotide sequence of the pgk-2 gene suggests that it arose from pgk-1 more than 100 million years ago by RNA-mediated gene duplication. The pgk-2 gene may, then, be a transcribed retroposon. Thus, gene duplication by retroposition may have been used as a mechanism for evolutionary diversification.

scholarly journals Nucleotide sequence of the phosphoglycerate kinase gene fromBacillus megaterium

1990 ◽  
Vol 18 (21) ◽  
pp. 6423-6423 ◽  
Author(s):  
B.S. Schläpfer ◽  
C. Branlant ◽  
G. Branlant ◽  
H. Zuber
Keyword(s):  
Nucleotide Sequence ◽  
Phosphoglycerate Kinase ◽  
Kinase Gene ◽  
Phosphoglycerate Kinase Gene

scholarly journals Nucleotide sequence of the phosphoglycerate kinase gene from the extreme thermophile Thermus thermophilus. Comparison of the deduced amino acid sequence with that of the mesophilic yeast phosphoglycerate kinase

1988 ◽  
Vol 254 (2) ◽  
pp. 509-517 ◽  
Author(s):  
D Bowen ◽  
J A Littlechild ◽  
J E Fothergill ◽  
H C Watson ◽  
L Hall
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Amino Acid Sequence ◽  
Thermus Thermophilus ◽  
Phosphoglycerate Kinase ◽  
Amino Acid Residues ◽  
Extreme Thermophile ◽  
Kinase Gene ◽  
Reading Frame ◽  
Phosphoglycerate Kinase Gene

Using oligonucleotide probes derived from amino acid sequencing information, the structural gene for phosphoglycerate kinase from the extreme thermophile, Thermus thermophilus, was cloned in Escherichia coli and its complete nucleotide sequence determined. The gene consists of an open reading frame corresponding to a protein of 390 amino acid residues (calculated Mr 41,791) with an extreme bias for G or C (93.1%) in the codon third base position. Comparison of the deduced amino acid sequence with that of the corresponding mesophilic yeast enzyme indicated a number of significant differences. These are discussed in terms of the unusual codon bias and their possible role in enhanced protein thermal stability.

Demethylation of specific sites in the 5' region of the inactive X-linked human phosphoglycerate kinase gene correlates with the appearance of nuclease sensitivity and gene expression

1988 ◽  
Vol 8 (11) ◽  
pp. 4692-4699
Author(s):  
R S Hansen ◽  
N A Ellis ◽  
S M Gartler
Keyword(s):  
Cell Lines ◽  
X Chromosome ◽  
Transcriptional Activation ◽  
Hybrid Cell ◽  
Methylation Status ◽  
Phosphoglycerate Kinase ◽  
Kinase Gene ◽  
Inactive X Chromosome ◽  
Phosphoglycerate Kinase Gene ◽  
Hypoxanthine Guanine Phosphoribosyltransferase

X8/6T2, a hamster-human hybrid cell line which contains an inactive human X chromosome, was treated with 5-azacytidine and selected for derepression of hypoxanthine-guanine phosphoribosyltransferase. Clones were examined for coreactivation of the phosphoglycerate kinase gene (Pgk). Of 68 of these hybrids, approximately 20% expressed measurable human phosphoglycerate kinase (PGK) activity. A 600-base-pair region of the Pgk 5' CpG cluster was examined for the methylation status of eight CCGG sites (site 1 being 5'-most) in a number of PGK-negative and PGK-positive cell lines. The inactive X chromosome is normally methylated at all eight sites, and this was also true for the majority of X8/6T2 cells. However, several PGK-negative hybrids were demethylated in the site 3 to site 6 region. PGK activity correlated with demethylation at both sites 6 and 7. The data for PGK-positive and -negative hybrids indicate that demethylation at or near site 7 was necessary for reactivation of Pgk. Chromatin sensitivity to MspI digestion in the nuclei of male lymphoblastoid cells and several PGK-positive and PGK-negative hybrids was examined. PGK-positive cell lines were hypersensitive to digestion, while PGK-negative hybrids were resistant. Cleavage at sites 6 and 7 was observed in all PGK-positive cell lines at each MspI concentration examined. Sites 7 and 8 were less accessible to digestion than site 6. Cleavage in the site 2 to site 5 region was observable at the lowest MspI concentration. In most PGK-positive hybrids, a nonspecific endogenous nuclease detected the presence of a hypersensitive region spanning at least 450 base pairs, bounded at the 3' end near HpaII site 6. Nuclease hypersensitivity appears to be related to promoter activity, because sites 7 and 8 are in transcribed regions of the gene. These data indicate that specific sites within the CpG cluster have a dominant controlling influence over the Pgk promoter conformation and the transcriptional activation of Pgk.

Stimulation of Yeast 3-Phosphoglycerate Kinase Gene Promoter by Paraquat

2000 ◽  
Vol 270 (3) ◽  
pp. 1036-1040 ◽  
Author(s):  
Neville Vassallo ◽  
Dolores R. Galea ◽  
William H. Bannister ◽  
Rena Balzan
Keyword(s):  
Phosphoglycerate Kinase ◽  
Gene Promoter ◽  
Kinase Gene ◽  
Phosphoglycerate Kinase Gene ◽  
Stimulation Of
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