Complete cDNA sequence for rabbit muscle glycogen phosphorylase

Nakano, Kenichi; Hwang, Peter K.; Fletterick, Robert J.

doi:10.1016/0014-5793(86)80829-8

Cited by 72 publications

(21 citation statements)

References 12 publications

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“…More than 50 years of research on glycogen phosphorylase in eukaryotes has yielded a rich harvest of ideas and principles, and the glgP genes have been isolated from several eukaryotic organisms [1][2][3][4][5][6][7], but this enzyme is as yet unknown in prokaryotes. There are at least three glycogen-synthesizing enzymes of bacteria, glycogen synthase, branching enzyme, and ADPglucose pyrophosphorylase, which are the gefie products of glgA, gigB, and gigC, respectively [8][9][10][11].…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and sequencing of the glycogen phosphorylase gene from Escherichia coli

Choi¹,

Kawamukai²,

Utsumi³

et al. 1989

FEBS Letters

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The glgP gene, which codes for glycogen phosphorylase, was cloned from a genomic library of Escherichia coil The nucleotide sequence of the glgP gene contained a single open reading frame encoding a protein consisting of 790 amino acid residues. The glgP gene product, a polypeptide of Mr 87 000, was confirmed by SDS-polyacrylamide gel electrophoresis. The deduced amino acid sequence showed that homology between glgP of E. carl and rabbit glgP, human glgP, potato glgP, and E. coli malP was 48.6, 48.6, 42.3, and 46.1%, respectively. Within this homologous region, the active site, glycogen storage site, and pyridoxal-5'-phosphate binding site are well conserved. The enzyme activity of glycogen phosphorylase increased after introduction on a multicopy of the glgP gene.

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Section: Introductionmentioning

confidence: 99%

Molecular cloning and sequencing of the glycogen phosphorylase gene from Escherichia coli

Choi¹,

Kawamukai²,

Utsumi³

et al. 1989

FEBS Letters

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“…4). The muscle form is the best characterized; both the primary sequence and the x-ray structure of rabbit muscle phosphorylase are known (5)(6)(7)(8). The enzyme functions in muscle to provide glucose required for the energy of contraction.…”

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confidence: 99%

“…Further, such comparisons could ultimately provide insight into how the phosphorylase genes, and perhaps other multigene families, are regulated in a developmental and tissue-specific manner. We have described the cloning and sequencing ofthe rabbit muscle glycogen phosphorylase cDNA and portions of the C-terminal domain from human and rat muscle (6,7). We report here the cDNA sequence and the deduced amino acid sequence for human liver glycogen phosphorylase.…”

mentioning

confidence: 99%

Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage.

Newgard¹,

Nakano²,

Hwang³

et al. 1986

Proc. Natl. Acad. Sci. U.S.A.

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We have cloned the cD)NA encoding glycogen phosphorylase (1,4-a-D-glucan:orthophosphate a-D-glucosyltransferase, EC 2.4.1.1) from human liver. Blot-hybridization analysis using a large fragment of the cDNA to probe mRNA from rabbit brain, muscle, and liver tissues shows preferential hybridization to liver RNA. Determination of the entire qucleotide sequence of the liver message has allowed a comparison with the previously determined rabbit muscle phosphorylase sequence. Despite an amino acid identity of 80%, the two cDNAs exhibit a remarkable divergence in G+C content. In the muscle phosphorylase sequence, 86% of the nucleotides at the third codon position are either deoxyguanosine or deoxycytidine residues, while in the liver homolog the figure is only 60%, resulting in a strikingly different pattern of codon usage throughout most of the sequence. The liver phosphorylase cDNA appears to represent an evolutionary mosaic; the segment encoding the N-terminal 80 amino acids contains >90% G+C at the third codon position. A survey of other published mammalian cDNA sequences reveals that the data for liver and muscle phosphorylases reflects a bias in codon usage patterns in liver and muscle coding sequences in general.Glycogen phosphorylase (1,4-a-D-glucan:orthophosphate a-D-glucosyltransferase, EC 2.4.1.1) isozymes play a vital role in mobilization of stored sugar in a variety of mammalian tissues. Three forms of the enzyme have been described that are distinguished by their electrophoretic mobilities on gels and their immunological properties (1-3). The three isozymes are tissue-specific; the brain type (also known as the fetal type) is predominant in adult brain and embryonic tissues, while the liver and muscle types are predominant in adult liver and skeletal muscle tissues, respectively (reviewed in ref. 4). The muscle form is the best characterized; both the primary sequence and the x-ray structure of rabbit muscle phosphorylase are known (5-8). The enzyme functions in muscle to provide glucose required for the energy of contraction. Its physiological role is distinct from the liver isozyme, which is centrally involved in the maintenance of blood glucose homeostasis, and from the brain form, which is associated primarily with provision of an emergency glucose supply during brief periods of anoxia or hypoglycemia (4, 9).Comparisons of the protein and DNA sequences of the phosphorylase isozymes are required to understand the evolutionary and functional relationships among them. Further, such comparisons could ultimately provide insight into how the phosphorylase genes, and perhaps other multigene families, are regulated in a developmental and tissue-specific manner. We have described the cloning and sequencing ofthe rabbit muscle glycogen phosphorylase cDNA and portions of the C-terminal domain from human and rat muscle (6, 7). We report here the cDNA sequence and the deduced amino acid sequence for human liver glycogen phosphorylase. Comparison of liver and muscle phosphorylase sequences reveals extensive...

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“…The entire aa sequence of M. haptotylum phosphorylase (gph1) showed 59 % identity to the S. cerevisiae glycogen phosphorylase and 45 % identity to rabbit muscle glycogen phosphorylase (Nakano et al, 1986). Multiple sequence alignment showed extensive sequence similarity in regions corresponding to the catalytic domain and C-terminal domain, while the regulatory or N-terminal domain appeared more variable ( Supplementary Fig.…”

Section: Glycogen and Carbon Metabolismmentioning

confidence: 99%

Comparison of gene expression in trap cells and vegetative hyphae of the nematophagous fungus Monacrosporium haptotylum

et al. 2005

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Nematode-trapping fungi enter the parasitic stage by developing specific morphological structures called traps. The global patterns of gene expression in traps and mycelium of the fungus Monacrosporium haptotylum were compared. The trap of this fungus is a unicellular spherical structure called the knob, which develops on the apex of a hyphal branch. RNA was isolated from knobs and mycelium and hybridized to a cDNA array containing probes of 2822 EST clones of M. haptotylum. Despite the fact that the knobs and mycelium were grown in the same medium, there were substantial differences in the patterns of genes expressed in the two cell types. In total, 23?3 % (657 of 2822) of the putative genes were differentially expressed in knobs versus mycelium. Several of these genes displayed sequence similarities to genes known to be involved in regulating morphogenesis and cell polarity in fungi. Among them were several putative homologues for small GTPases, such as rho1, rac1 and ras1, and a rho GDP dissociation inhibitor (rdi1). Several homologues to genes involved in stress response, protein synthesis and protein degradation, transcription, and carbon metabolism were also differentially expressed. In the last category, a glycogen phosphorylase (gph1) gene homologue, one of the most upregulated genes in the knobs as compared to mycelium, was characterized. A number of the genes that were differentially expressed in trap cells are also known to be regulated during the development of infection structures in plant-pathogenic fungi. Among them, a gas1 (mas3) gene homologue (designated gks1), which is specifically expressed in appressoria of the rice blast fungus, was characterized.

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Complete cDNA sequence for rabbit muscle glycogen phosphorylase

Cited by 72 publications

References 12 publications

Molecular cloning and sequencing of the glycogen phosphorylase gene from Escherichia coli

Molecular cloning and sequencing of the glycogen phosphorylase gene from Escherichia coli

Sequence analysis of the cDNA encoding human liver glycogen phosphorylase reveals tissue-specific codon usage.

Comparison of gene expression in trap cells and vegetative hyphae of the nematophagous fungus Monacrosporium haptotylum

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