scholarly journals Structural analysis of mutant and revertant forms of Chinese hamster hypoxanthine-guanine phosphoribosyltransferase.

1981 ◽  
Vol 256 (6) ◽  
pp. 2878-2886
Author(s):  
G.D. Kruh ◽  
R.G. Fenwick ◽  
C.T. Caskey
Keyword(s):  
Structural Analysis ◽  
Chinese Hamster ◽  
Hypoxanthine Guanine Phosphoribosyltransferase

scholarly journals 8-AZAGUANINE RESISTANCE IN MAMMALIAN CELLS I. HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE

Genetics ◽  
1972 ◽  
Vol 72 (2) ◽  
pp. 239-252 ◽  
Author(s):  
F D Gillin ◽  
D J Roufa ◽  
A L Beaudet ◽  
C T Caskey
Keyword(s):  
Nucleic Acid ◽  
Mammalian Cells ◽  
Chinese Hamster ◽  
Acid Synthesis ◽  
Ethyl Methanesulfonate ◽  
Nucleic Acid Synthesis ◽  
Wild Type ◽  
Chinese Hamster Cells ◽  
Hypoxanthine Guanine Phosphoribosyltransferase

ABSTRACT Chinese hamster cells were treated with ethyl methanesulfonate or N-methyl-N'-nitro-N-nitrosoguanidine, and mutants resistant to 8-azaguanine were selected and characterized. Hypoxanthine-guanine phosphoribosyltransferase activity of sixteen mutants is extremely negative, making them suitable for reversion to HGPRTase+. Ten of the extremely negative mutants revert at a frequency higher than 10-7 suggesting their point mutational character. The remaining mutants have demonstrable HGPRTase activity and are not useful for reversion analysis. Five of these mutants have < 2% HGPRTase and are presumably also HGPRTase point mutants. The remaining 14 mutants utilize exogenous hypoxanthine for nucleic acid synthesis poorly, and possess 20-150% of wild-type HGPRTase activity in in vitro. Their mechanism of 8-azaguanine resistance is not yet defined.

scholarly journals Hypoxanthine-guanine phosphoribosyltransferase genes of mouse and Chinese hamster: construction and sequence analysis of cDNA recombinants

1982 ◽  
Vol 10 (21) ◽  
pp. 6763-6775 ◽  
Author(s):  
David S. Konecki ◽  
John Brennand ◽  
James C. Fuscoe ◽  
C.Thomas Caskey ◽  
A.Craig Chinault
Keyword(s):  
Sequence Analysis ◽  
Chinese Hamster ◽  
Hypoxanthine Guanine Phosphoribosyltransferase

Molecular Structural Analysis ofHPRTMutations Induced by Thermal and Epithermal Neutrons in Chinese Hamster Ovary Cells

2000 ◽  
Vol 154 (3) ◽  
pp. 313-318 ◽  
Author(s):  
Yuko Kinashi ◽  
Yoshinori Sakurai ◽  
Shinichiro Masunaga ◽  
Minoru Suzuki ◽  
Masao Takagaki ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Ovary Cells ◽  
Epithermal Neutrons

scholarly journals Deletion and amplification of the HGPRT locus in Chinese hamster cells.

1983 ◽  
Vol 3 (6) ◽  
pp. 1086-1096 ◽  
Author(s):  
J C Fuscoe ◽  
R G Fenwick ◽  
D H Ledbetter ◽  
C T Caskey
Keyword(s):  
Molecular Mechanisms ◽  
Cdna Probe ◽  
Chinese Hamster ◽  
Chinese Hamster Cell ◽  
Linked Gene ◽  
Translocation Event ◽  
Cytogenetic Studies ◽  
Dna Deletions ◽  
Hypoxanthine Guanine Phosphoribosyltransferase ◽  
Cloned Cdna

Somatic cell selective techniques and hybridization analyses with a cloned cDNA probe were used to isolate and identify Chinese hamster cell lines in which the X-linked gene for hypoxanthine-guanine phosphoribosyltransferase (HGPRT) has been altered. Two of 19 HGPRT-deficient mutants selected were found to have major DNA deletions affecting the HGPRT locus. Cytogenetic studies revealed that the X chromosome of each deletion mutant had undergone a translocation event, whereas those from the remaining 17 mutants were normal. Phenotypic revertants of the thermosensitive HGPRT mutant RJK526 were isolated, and amplification of the mutant allele was shown to be the predominant mechanism of reversion. Comparisons of restriction enzyme fragments of DNA from deletion versus amplification strains identified two regions of the Chinese hamster genome that contained homology to the cDNA probe. One was shown to be much larger than the 1,600-nucleotide mRNA for HGPRT and to be comprised of linked fragments that contained the functional HGPRT gene. The second was neither transcribed nor tightly linked to the functional gene. These initial studies of HGPRT alterations at the level of DNA thus identified molecular mechanisms of phenotypic variation.

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