Complete sequence of the chicken glyceraldehyde-3-phosphate dehydrogenase gene.

Stone, Edwin M.; Rothblum, Katrina; Alevy, Martin C.; Kuo, Tien; Schwartz, Robert J.

doi:10.1073/pnas.82.6.1628

Cited by 95 publications

(43 citation statements)

References 26 publications

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“…This gene was sequenced, and it was found to contain a coding sequence of 993 nucleotides coding for a 331-aminoacid polypeptide. The coding region shows significant homology (78 to 79%) with the S. cerevisiae TDH1-3 genes and also with the chicken GAPDH gene (67%) (50). Comparison of the amino acid sequences indicates a high degree of identity to the S. cerevisiae (76%) and the chicken (67%) proteins.…”

Section: Resultsmentioning

confidence: 87%

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

et al. 1997

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A gt11 cDNA library from Candida albicans ATCC 26555 was screened by using pooled sera from two patients with systemic candidiasis and five neutropenic patients with high levels of anti-C. albicans immunoglobulin M antibodies. Seven clones were isolated from 60,000 recombinant phages. The most reactive one contained a 0.9-kb cDNA encoding a polypeptide immunoreactive only with sera from patients with systemic candidiasis. The whole gene was isolated from a genomic library by using the cDNA as a probe. The nucleotide sequence of the coding region showed homology (78 to 79%) to the Saccharomyces cerevisiae TDH1 to TDH3 genes coding for glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and their amino acid sequences showed 76% identity; thus, this gene has been named C. albicans TDH1. A rabbit polyclonal antiserum against the purified cytosolic C. albicans GAPDH (polyclonal antibody [PAb] anti-CA-GAPDH) was used to identify the GAPDH in the ␤-mercaptoethanol extracts containing cell wall moieties. Indirect immunofluorescence demonstrated the presence of GAPDH at the C. albicans cell surface, particularly on the blastoconidia. Semiquantitative flow cytometry analysis showed the sensitivity of this GAPDH form to trypsin and its resistance to be removed with 2 M NaCl or 2% sodium dodecyl sulfate. The decrease in fluorescence in the presence of soluble GAPDH indicates the specificity of the labelling. In addition, a dose-dependent GAPDH enzymatic activity was detected in intact blastoconidia and germ tube cells. This activity was reduced by pretreatment of the cells with trypsin, formaldehyde, and PAb anti-CA-GAPDH. These observations indicate that an immunogenic, enzymatically active cell wall-associated form of the glycolytic enzyme GAPDH is found at the cell surface of C. albicans cells.

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Section: Resultsmentioning

confidence: 87%

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

et al. 1997

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“…In addition to the three rp genes described here, it has also been observed for a few viral (2) and cellular (5,20,23,41,51) genes. Interestingly, most of these cellular genes are also of the housekeeping category and share sequence features with the rp genes, e.g., the pyrimidine motif at or near to the cap site (20,23,41,77) or the neighboring C+G-rich blocks (5,20,51,77). Other housekeeping genes with C + G-rich 5' regions that lack a canonical TATA box have been described previously (12,63,90).…”

Section: Discussionmentioning

confidence: 99%

Characterization of the multigene family encoding the mouse S16 ribosomal protein: strategy for distinguishing an expressed gene from its processed pseudogene counterparts by an analysis of total genomic DNA.

Wagner¹,

Perry²

1985

Mol. Cell. Biol.

184

114

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Two genes from the family encoding mouse ribosomal protein S16 were cloned, sequenced, and analyzed. One gene was found to be a processed pseudogene, i.e., a nonfunctional gene presumably derived from an mRNA intermediate. The other S16 gene contained introns and had exonic sequences identical to those of a cloned S16 cDNA. The expression of this gene was demonstrated by Northern blot analysis of nuclear poly(A)+ RNA with cDNA and unique sequence intron probes. Each S16 intron contains a well-preserved remnant of the TACTAAC motif, which is ubiquitous in yeast introns and known to play a critical role in intron splicing. A sequence comparison with two other mouse ribosomal protein genes analyzed in our laboratory, L30 and L32, revealed common structural features which might be involved in the control and coordination of ribosomal protein gene expression. These include the lack of a canonical TATA box in the -20 to -30 region and a remarkably similar 12-nucleotide pyrimidine sequence (CTTCCYTYYTC) that spans the cap site and is flanked by C + G-rich sequences. The nature of the other members of the S16 family was evaluated by three types of experiment: a DNase I sensitivity analysis to measure the extent of chromatin condensation; an analysis of the thermal stability of cDNA-gene hybrids to estimate the extent of divergence of each gene sequence from that of the expressed gene; and a restriction fragment analysis which distinguishes intron-containing genes from intronless processed genes. The results of these analyses show (i) that all genes except the expressed S16 gene are in a condensed chromatin configuration associated with transcriptional quiescence; (ii) that most of the genes within the S16 family have sequences >7% divergent from the expressed S16 gene; and (iii) that at least 7 of the 10 S16 genes lack introns. We conclude that the ribosomal protein S16 multigene family contains one expressed intron-containing gene and nine inactive pseudogenes, most or all of which are of the processed type.The eucaryotic ribosome is a complex organelle composed of four RNA species and over 70 different proteins. The biosynthesis of these various components is coordinately regulated during embryonic development and in response to changes in cell growth rate by a variety of mechanisms operating at several levels of gene expression (21,27,36,52,59,62). To understand how these mechanisms operate in higher eucaryotes it is important to know how the individual genes are organized and expressed. While there is considerable knowledge of the structure and expression of the rRNA genes of higher eucaryotes, much less is known about the ribosomal protein (rp) genes.Our earlier investigations revealed that the sequences encoding individual rps are present in mammalian genomes as multigene families containing 10 to 25 members (55). Initially, this great multiplicity of rp genes seemed to present a daunting obstacle to those wishing to understand the genetic basis of how mammalian rp genes are coordinately regulated. However, the re...

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“…The DNA probe used to detect the vIL-8 transcript was PCR amplified from the genomic DNA of MSB-1 cells, using primers vIL8B1 and vIL8F4. DNA probes for meq and chicken glyceraldehyde-3-phosphate dehydrogenase (GAPDH) were from respective subclones as described previously (63).…”

Section: Cells and Viruses Msb-1 Cells (3)mentioning

confidence: 99%

Marek's Disease Virus (MDV) Encodes an Interleukin-8 Homolog (vIL-8): Characterization of the vIL-8 Protein and a vIL-8 Deletion Mutant MDV

Parcells

Lin

Dienglewicz

et al. 2001

J Virol

155

134

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Chemokines induce chemotaxis, cell migration, and inflammatory responses. We report the identification of an interleukin-8 (IL-8) homolog, termed vIL-8, encoded within the genome of Marek's disease virus (MDV).The 134-amino-acid vIL-8 shares closest homology to mammalian and avian IL-8, molecules representing the prototype CXC chemokine. The gene for vIL-8 consists of three exons which map to the BamHI-L fragment within the repeats flanking the unique long region of the MDV genome. A 0.7-kb transcript encoding vIL-8 was detected in an n-butyrate-treated, MDV-transformed T-lymphoblastoid cell line, MSB-1. This induction is essentially abolished by cycloheximide and herpesvirus DNA polymerase inhibitor phosphonoacetate, indicating that vIL-8 is expressed with true late (␥ 2 ) kinetics. Baculovirus-expressed vIL-8 was found to be secreted into the medium and shown to be functional as a chemoattractant for chicken peripheral blood mononuclear cells but not for heterophils. To characterize the function of vIL-8 with respect to MDV infection in vivo, a recombinant MDV was constructed with a deletion of all three exons and a soluble-modified green fluorescent protein (smGFP) expression cassette inserted at the site of deletion. In two in vivo experiments, the vIL-8 deletion mutant (RB1BvIL-8⌬smGFP) showed a decreased level of lytic infection in comparison to its parent virus, an equal-passage-level parent virus, and to another recombinant MDV containing the insertion of a GFP expression cassette at the nonessential US2 gene. RB1BvIL-8⌬smGFP retained oncogenicity, albeit at a greatly reduced level. Nonetheless, we have been able to establish a lymphoblastoid cell line from an RB1BvIL-8⌬smGFP-induced ovarian lymphoma (MDCC-UA20) and verify the presence of a latent MDV genome lacking vIL-8. Taken together, these data describe the identification and characterization of a chemokine homolog encoded within the MDV genome that is dispensable for transformation but may affect the level of MDV in vivo lytic infection.

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Complete sequence of the chicken glyceraldehyde-3-phosphate dehydrogenase gene.

Cited by 95 publications

References 26 publications

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen

Characterization of the multigene family encoding the mouse S16 ribosomal protein: strategy for distinguishing an expressed gene from its processed pseudogene counterparts by an analysis of total genomic DNA.

Marek's Disease Virus (MDV) Encodes an Interleukin-8 Homolog (vIL-8): Characterization of the vIL-8 Protein and a vIL-8 Deletion Mutant MDV

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