scholarly journals A Distal Mutation Perturbs Dynamic Amino Acid Networks in Dihydrofolate Reductase

Biochemistry ◽  
2013 ◽  
Vol 52 (27) ◽  
pp. 4605-4619 ◽  
Author(s):  
David D. Boehr ◽  
Jason R. Schnell ◽  
Dan McElheny ◽  
Sung-Hun Bae ◽  
Brendan M. Duggan ◽  
...  
Keyword(s):  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Distal Mutation

scholarly journals Characterization and amino acid sequence of Neisseria gonorrhoeae dihydrofolate reductase.

1984 ◽  
Vol 259 (19) ◽  
pp. 12291-12298 ◽  
Author(s):  
D P Baccanari ◽  
R L Tansik ◽  
S J Paterson ◽  
D Stone
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neisseria Gonorrhoeae ◽  
Dihydrofolate Reductase

A single amino acid substitution in Staphylococcus aureus dihydrofolate reductase determines trimethoprim resistance 1 1 Edited by T.Richmond

1997 ◽  
Vol 266 (1) ◽  
pp. 23-30 ◽  
Author(s):  
Glenn E. Dale ◽  
Clemens Broger ◽  
Allan D' Arcy ◽  
Peter G. Hartman ◽  
Ronald DeHoogt ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Amino Acid Substitution ◽  
Single Amino Acid Substitution ◽  
Single Amino Acid

Spontaneous splicing mutations at the dihydrofolate reductase locus in Chinese hamster ovary cells

1986 ◽  
Vol 6 (6) ◽  
pp. 1926-1935
Author(s):  
P J Mitchell ◽  
G Urlaub ◽  
L Chasin
Keyword(s):  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Splice Site ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster Ovary Cells ◽  
Chinese Hamster ◽  
Splice Sites ◽  
Ovary Cells ◽  
Splicing Mutations ◽  
Intron 4

We isolated and characterized three spontaneous mutants of Chinese hamster ovary cells that were deficient in dihydrofolate reductase activity. All three mutants contained no detectable enzyme activity and produced dihydrofolate reductase mRNA species that were shorter than those of the wild type by about 120 bases. Six exons are normally represented in this mRNA; exon 5 was missing in all three mutant mRNAs. Nuclease S1 analysis of the three mutants indicated that during the processing of the mutant RNA, exon 4 was spliced to exon 6. The three mutant genes were cloned, and the regions around exons 4 and 5 were sequenced. In one mutant, the GT dinucleotide at the 5' end of intron 5 had changed to CT. In a second mutant, the first base in exon 5 had changed from G to T. In a revertant of this mutant, this base was further mutated to A, a return to a purine. Approximately 25% of the mRNA molecules in the revertant were spliced correctly to produce an enzyme with one presumed amino acid change. In the third mutant, the AG at the 3' end of intron 4 had changed to AA. A mutation that partially reversed the mutant phenotype had changed the dinucleotide at the 5' end of intron 4 from GT to AT. The splicing pattern in this revertant was consistent with the use of cryptic donor and acceptor splice sites close to the original sites to produce an mRNA with three base changes and a protein with two amino acid changes. These mutations argue against a scanning model for the selection of splice site pairs and suggest that only a single splice site need be inactivated to bring about efficient exon skipping (a regulatory mechanism for some genes). The fact that all three mutants analyzed exhibited exon 5 splicing mutations indicates that these splice sites are hot spots for spontaneous mutation.

Sequence Perturbation Analysis: Addressing Amino Acid Indices to Elucidate the C-Terminal Role of Escherichia Coli Dihydrofolate Reductase

2009 ◽  
Vol 145 (6) ◽  
pp. 751-762 ◽  
Author(s):  
Hisashi Takahashi ◽  
Akiko Yokota ◽  
Tatsuyuki Takenawa ◽  
Masahiro Iwakura
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Perturbation Analysis ◽  
Amino Acid Indices

scholarly journals A Conservative Amino Acid Mutation in the Chromosome‐Encoded Dihydrofolate Reductase Confers Trimethoprim Resistance inStreptococcus pneumoniae

1998 ◽  
Vol 178 (3) ◽  
pp. 700-706 ◽  
Author(s):  
Andreas Pikis ◽  
Jacob A. Donkersloot ◽  
William J. Rodriguez ◽  
Jerry M. Keith
Keyword(s):  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Amino Acid Mutation

scholarly journals Amino acid changes linked to pyrimethamine resistance in the dihydrofolate reductase-thymidylate synthase gene of Plasmodium falciparum.

1988 ◽  
Vol 85 (23) ◽  
pp. 9109-9113 ◽  
Author(s):  
A. F. Cowman ◽  
M. J. Morry ◽  
B. A. Biggs ◽  
G. A. Cross ◽  
S. J. Foote
Keyword(s):  
Plasmodium Falciparum ◽  
Amino Acid ◽  
Dihydrofolate Reductase ◽  
Thymidylate Synthase

Photoaffinity analogs of methotrexate as folate antagonist binding probes. 1. Photoaffinity labeling of murine L1210 dihydrofolate reductase and amino acid sequence of the binding region

Biochemistry ◽  
1987 ◽  
Vol 26 (15) ◽  
pp. 4751-4756 ◽  
Author(s):  
Elmer M. Price ◽  
Philip L. Smith ◽  
Teri E. Klein ◽  
James H. Freisheim
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Dihydrofolate Reductase ◽  
Photoaffinity Labeling ◽  
Binding Region ◽  
Antagonist Binding
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