Backbone Amide Dynamics Studies of Apo-L75F-TrpR, a Temperature-Sensitive Mutant of the Tryptophan Repressor Protein (TrpR): Comparison with the15N NMR Relaxation Profiles of Wild-Type and A77V Mutant Apo-TrpR Repressors

Biochemistry ◽  
2010 ◽  
Vol 49 (37) ◽  
pp. 8006-8019 ◽  
Author(s):  
Anupam Goel ◽  
Brian P. Tripet ◽  
Robert C. Tyler ◽  
Lucas D. Nebert ◽  
Valérie Copié
Keyword(s):  
Nmr Relaxation ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Sensitive Mutant ◽  
Repressor Protein ◽  
Temperature Sensitive Mutant ◽  
Backbone Amide ◽  
Tryptophan Repressor

scholarly journals Dynamical Studies Of A Temperature-Sensitive Mutant Of The Tryptophan Repressor Protein, L75F-TrpR

2009 ◽  
Vol 96 (3) ◽  
pp. 322a
Author(s):  
Valerie Copie ◽  
Brian Tripet ◽  
Anupam Goel ◽  
Lucas Nerbert ◽  
Jannette Carey
Keyword(s):  
Temperature Sensitive ◽  
Sensitive Mutant ◽  
Repressor Protein ◽  
Temperature Sensitive Mutant ◽  
Tryptophan Repressor

A dominant temperature-sensitive assembly mutant of adenovirus type 2

1979 ◽  
Vol 25 (5) ◽  
pp. 646-649 ◽  
Author(s):  
Eric B. Carstens ◽  
Johanne Magnan ◽  
Joseph Weber
Keyword(s):  
Negative Temperature ◽  
Adenovirus Type ◽  
Wild Type Virus ◽  
Temperature Sensitive ◽  
Nonpermissive Temperature ◽  
Wild Type ◽  
Sensitive Mutant ◽  
Virion Assembly ◽  
Temperature Sensitive Mutant

An assembly negative temperature-sensitive mutant of Ad2, ts48 was shown to exert dominance over other ts mutants and wild-type virus during coinfection, by inhibiting virion assembly. Dominance was only expressed at the nonpermissive temperature.

scholarly journals Genetics of nitrate reductase inUstilago maydis

1970 ◽  
Vol 16 (2) ◽  
pp. 151-163 ◽  
Author(s):  
C. M. Lewis ◽  
J. R. S. Fincham
Keyword(s):  
Nitrate Reductase ◽  
Structural Gene ◽  
Nitrate Reduction ◽  
Ustilago Maydis ◽  
Xanthine Dehydrogenase ◽  
Temperature Sensitive ◽  
Wild Type ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Complementation Groups

SUMMARYMutants ofUstilago maydishave been isolated both, deficient and derepressed for nitrate reduction. Those deficient in enzyme fall into six groups, one of which is the structural gene. Enzyme which has proved to be more labile than that of wild-type has been isolated from a temperature-sensitive mutant at this locus. All the mutants in the structural gene have xanthine dehydrogenase activity and the situation closely parallels that ofAspergillus nidulans.The derepressed mutants fall into four complementation groups and all are partially derepressed in that they are further inducible by nitrate. Full derepression can be conferred by induction of a second mutation. In one analysed case the second reinforcing mutation proved to be pheno-typically similar to the first one when separated from it.

scholarly journals Nontransmissible Virus-Like Particle Formation by F-Deficient Sendai Virus Is Temperature Sensitive and Reduced by Mutations in M and HN Proteins

2003 ◽  
Vol 77 (5) ◽  
pp. 3238-3246 ◽  
Author(s):  
Makoto Inoue ◽  
Yumiko Tokusumi ◽  
Hiroshi Ban ◽  
Takumi Kanaya ◽  
Tsuyoshi Tokusumi ◽  
...  
Keyword(s):  
Gene Expression ◽  
Sendai Virus ◽  
M Protein ◽  
Temperature Sensitive ◽  
Amino Acid Substitutions ◽  
Wild Type ◽  
Sensitive Mutant ◽  
Temperature Sensitive Mutant ◽  
Virus Like Particle ◽  
Infected Cells

ABSTRACT The formation of nontransmissible virus-like particles (NTVLP) by cells infected with F-deficient Sendai virus (SeV/ΔF) was found to be temperature sensitive. Analysis by hemagglutination assays and Western blotting demonstrated that the formation of NTVLP at 38°C was about 1/100 of that at 32°C, whereas this temperature-sensitive difference was only moderate in the case of F-possessing wild-type SeV. In order to reduce the NTVLP formation with the aim of improving SeV for use as a vector for gene therapy, amino acid substitutions found in temperature-sensitive mutant SeVs were introduced into the M (G69E, T116A, and A183S) and HN (A262T, G264R, and K461G) proteins of SeV/ΔF to generate SeV/MtsHNtsΔF. The use of these mutations allows vector production at low temperature (32°C) and therapeutic use at body temperature (37°C) with diminished NTVLP formation. As expected, the formation of NTVLP by SeV/MtsHNtsΔF at 37°C was decreased to about 1/10 of that by SeV/ΔF, whereas the suppression of NTVLP formation did not cause either enhanced cytotoxicity or reduced gene expression of the vector. The vectors showed differences with respect to the subcellular distribution of M protein in the infected cells. Clear and accumulated immunocytochemical signals of M protein on the cell surface were not observed in cells infected by SeV/ΔF at an incompatible temperature, 38°C, or in those infected by SeV/MtsHNtsΔF at 37 or 38°C. The absence of F protein in SeV/ΔF and the additional mutations in M and HN in SeV/MtsHNtsΔF probably weaken the ability to transport M protein to the plasma membrane, leading to the diminished formation of NTVLP.

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