Sequence Analysis of X-Ray-Induced Mutations Occurring in a cDNA of the Human hprt Gene Integrated into Mammalian Chromosomal DNA

1993 ◽  
Vol 134 (2) ◽  
pp. 202 ◽  
Author(s):  
Hiroshi Kimura ◽  
Hirofumi Higuchi ◽  
Hiroaki Iyehara-Ogawa ◽  
Takesi Kato
Keyword(s):  
Sequence Analysis ◽  
Induced Mutations ◽  
Chromosomal Dna ◽  
Hprt Gene ◽  
X Ray ◽  
Human Hprt Gene

Spectrum of X-ray-induced mutations in the human hprt gene

1994 ◽  
Vol 15 (3) ◽  
pp. 495-502 ◽  
Author(s):  
Stephen L. Nelson ◽  
Cynthia R. Giver ◽  
Andrew J. Grosovsky
Keyword(s):  
Induced Mutations ◽  
Hprt Gene ◽  
X Ray ◽  
Human Hprt Gene

Spectrum of spontaneous mutations in a cDNA of the human hprt gene integrated in chromosomal DNA

1989 ◽  
Vol 219 (3) ◽  
pp. 349-358 ◽  
Author(s):  
Hironobu Ikehata ◽  
Toshiaki Akagi ◽  
Hiroshi Kimura ◽  
Susumu Akasaka ◽  
Takesi Kato
Keyword(s):  
Spontaneous Mutations ◽  
Chromosomal Dna ◽  
Hprt Gene ◽  
Human Hprt Gene

DNA sequence analysis of 1-nitrosopyrene-induced mutations in the hprt gene of Chinese hamster ovary cells

1992 ◽  
Vol 13 (5) ◽  
pp. 819-825 ◽  
Author(s):  
Ronald K. Newton ◽  
Robert A. Mittelstaedt ◽  
Mugimane.G. Manjanatha ◽  
Robert.H. Heflich
Keyword(s):  
Sequence Analysis ◽  
Dna Sequence ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Dna Sequence Analysis ◽  
Induced Mutations ◽  
Hprt Gene ◽  
Ovary Cells

Developing structure-based models to predict substrate specificity of D-group (Type II) molybdenum enzymes: application to a molybdo-enzyme of unknown function from Archaeoglobus fulgidus

2006 ◽  
Vol 34 (1) ◽  
pp. 118-121 ◽  
Author(s):  
E.J. Dridge ◽  
D.J. Richardson ◽  
R.J. Lewis ◽  
C.S. Butler
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Archaeoglobus Fulgidus ◽  
Substrate Selectivity ◽  
Type Ii ◽  
Amino Acid Residues ◽  
Sequence Alignments ◽  
X Ray ◽  
Group Type

The AF0174–AF0176 gene cluster in Archaeoglobus fulgidus encodes a putative oxyanion reductase of the D-type (Type II) family of molybdo-enzymes. Sequence analysis reveals that the catalytic subunit AF0176 shares low identity (31–32%) and similarity (41–42%) to both NarG and SerA, the catalytic components of the respiratory nitrate and selenate reductases respectively. Consequently, predicting the oxyanion substrate selectivity of AF0176 has proved difficult based solely on sequence alignments. In the present study, we have modelled both AF0176 and SerA on the recently determined X-ray structure of the NAR (nitrate reductase) from Escherichia coli and have identified a number of key amino acid residues, conserved in all known NAR sequences, including AF0176, that we speculate may enhance selectivity towards trigonal planar (NO3−) rather than tetrahedral (SeO42− and ClO4−) substrates.

Functional characterization of the human hypoxanthine phosphoribosyltransferase gene promoter: evidence for a negative regulatory element

1991 ◽  
Vol 11 (8) ◽  
pp. 4157-4164
Author(s):  
D E Rincón-Limas ◽  
D A Krueger ◽  
P I Patel
Keyword(s):  
Regulatory Element ◽  
Genomic Structure ◽  
Functional Characterization ◽  
Translation Initiation Site ◽  
Hypoxanthine Phosphoribosyltransferase ◽  
Hprt Gene ◽  
Negative Element ◽  
Cis Acting ◽  
Human Hprt Gene

The enzyme hypoxanthine phosphoribosyltransferase (HPRT) catalyzes the metabolic salvage of the purine bases hypoxanthine and guanine. We previously characterized the genomic structure of the human HPRT gene and described its promoter sequence. In this report, we identify cis-acting transcriptional control regions of the human HPRT gene by linking various 5'-flanking sequences to the bacterial chloramphenicol acetyltransferase gene. The sequence from positions -219 to -122 relative to the translation initiation site is required for maximal expression of this gene, and it functions equally in both normal and reverse orientations. In addition, a cis-acting negative element is present in the region spanning from positions -570 to -388. This negative element can also repress promoters of heterologous genes, such as those of adenosine deaminase and dihydrofolate reductase, which are structurally and functionally similar to the human HPRT promoter. Furthermore, this repressor element functions independently of its orientation but appears to be distance dependent. In vivo competition assays demonstrated that the trans-acting factor(s) that binds to this negative element specifically inhibits human HPRT promoter activity. Taken together, these data localize cis-acting sequences important in the regulation of human HPRT gene expression and should allow the study of protein-DNA interactions which modulate the transcription of this gene.

X-RAY AND ULTRA-VIOLET INDUCED MUTATIONS IN NEUROSPORA*

1941 ◽  
Vol 32 (11) ◽  
pp. 405-412 ◽  
Author(s):  
CARL C. LINDEGREN AND GERTRUDE LINDEGREN
Keyword(s):  
Ultra Violet ◽  
Induced Mutations ◽  
X Ray
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