Hydroxylamine mutagenesis solution

2006 ◽  
Vol 2006 (1) ◽  
pp. pdb.rec529
Keyword(s):  
Hydroxylamine Mutagenesis

scholarly journals ESCHERICHIA COLI RHO FACTOR IS INVOLVED IN LYSIS OF BACTERIOPHAGE T4-INFECTED CELLS

Genetics ◽  
1985 ◽  
Vol 111 (2) ◽  
pp. 197-218
Author(s):  
Claës H Linder ◽  
Karin Carlson
Keyword(s):  
Bacteriophage T4 ◽  
Growth Conditions ◽  
Plaque Formation ◽  
Early Gene ◽  
Multicopy Plasmid ◽  
Lysis Inhibition ◽  
Cold Sensitive ◽  
Phage Production ◽  
Hydroxylamine Mutagenesis ◽  
High Level

ABSTRACT A Rid (Rho interaction deficient) phenotype of bacteriophage T4 mutants was defined by cold-sensitive restriction (lack of plaque formation) on rho  + hosts carrying additional polar mutations in unrelated genes, coupled to suppression (plaque formation) in otherwise isogenic strains carrying either a polarity-suppressing rho or a multicopy plasmid expressing the rho  + allele. This suggests that the restriction may be due to lower levels of Rho than what is available to T4 in the suppressing strains.—Rid394×4 was isolated upon hydroxylamine mutagenesis and mapped in the t gene; other t mutants (and mot, as well as dda dexA double mutants) also showed a Rid phenotype. In liquid culture in strains that restricted plaque formation Rid394×4 showed strong lysis inhibition (a known t  - phenotype) but no prolonged phage production (another well-known t  - phenotype). This implies that when Rho is limiting the t mutant shuts off phage production at the normal time. Lysis inhibition was partially relieved, and phage production prolonged to varying extents depending on growth conditions in strains that allowed plaque formation. No significant effects on early gene expression were found. Apparently, both mutant (polarity-suppressing) and wild-type Rho can function in prolonging phage production and partially relieving lysis inhibition of Rid394×4 when present at a sufficiently high level, and Rho may play other role(s) in T4 development than in early gene regulation.

Hydroxylamine mutagenesis of HSV DNA and DNA fragments: Introduction of mutations into selected regions of the viral genome

Virology ◽  
1979 ◽  
Vol 98 (1) ◽  
pp. 168-181 ◽  
Author(s):  
Chien-Ts Chu ◽  
Deborah S. Parris ◽  
Richard A.F. Dixon ◽  
Florence E. Farber ◽  
Priscilla A. Schaffer
Keyword(s):  
Viral Genome ◽  
Dna Fragments ◽  
Hydroxylamine Mutagenesis

Mechanism of hydroxylamine mutagenesis: tautomeric shifts and proton exchange between the promutagen N6-methoxyadenosine and cytidine

Biochemistry ◽  
1987 ◽  
Vol 26 (14) ◽  
pp. 4332-4337 ◽  
Author(s):  
Ryszard Stolarski ◽  
Borys Kierdaszuk ◽  
Curt Eric Hagberg ◽  
David Shugar
Keyword(s):  
Proton Exchange ◽  
Hydroxylamine Mutagenesis

Conformation of exocyclic amino groups in purines and pyrimidines: crystal structure and conformation of 1-methyl-N4-hydroxycytosine hydrochloride

1979 ◽  
Vol 57 (4) ◽  
pp. 308-313 ◽  
Author(s):  
George I. Birnbaum ◽  
Tadeusz Kulikowski ◽  
David Shugar
Keyword(s):  
Crystal Structure ◽  
Direct Methods ◽  
Amino Groups ◽  
Neutral Form ◽  
Triclinic Space Group ◽  
Hydrochloride Salt ◽  
Cell Dimensions ◽  
Hydroxylamine Mutagenesis ◽  
Intramolecular Hydrogen ◽  
Purines And Pyrimidines

The hydrochloride salt of 1-methyl-N4-hydroxycytosine crystallizes in the triclinic space group [Formula: see text] with cell dimensions: a = 8.232(1), b = 9.293(1), c = 5.416(1) Å (1 Å = 0.1 nm); α = 91.95(1), β = 91.72(2), γ = 71.56(1)° (SE in parentheses). The structure was solved by direct methods and refined to R = 3.7% for 1514 reflections. Despite the absence of an intramolecular hydrogen bond in the solid state, the N4-hydroxy substituent is syn to the ring N(3). This conformation, which probably prevails also in the neutral form, is of relevance to the mechanism of attack of cytosine by hydroxylamine, known to involve predominantly the cytosine cation, as well as to the mechanism of hydroxylamine mutagenesis. Such conformational aspects are also relevant to other phenomena, including translation and restriction.

scholarly journals Assembly of 60S ribosomal subunits is perturbed in temperature-sensitive yeast mutants defective in ribosomal protein L16.

1991 ◽  
Vol 11 (11) ◽  
pp. 5681-5692 ◽  
Author(s):  
M Moritz ◽  
B A Pulaski ◽  
J L Woolford
Keyword(s):  
Translation Initiation ◽  
Ribosomal Subunit ◽  
Ribosome Assembly ◽  
Temperature Sensitive ◽  
Ribosomal Subunits ◽  
Temperature Sensitive Mutants ◽  
Ribosomal Subunit Protein ◽  
Cold Sensitive ◽  
Hydroxylamine Mutagenesis ◽  
Yeast Mutants

Temperature-sensitive mutants defective in 60S ribosomal subunit protein L16 of Saccharomyces cerevisiae were isolated through hydroxylamine mutagenesis of the RPL16B gene and plasmid shuffling. Two heat-sensitive and two cold-sensitive isolates were characterized. The growth of the four mutants is inhibited at their restrictive temperatures. However, many of the cells remain viable if returned to their permissive temperatures. All of the mutants are deficient in 60S ribosomal subunits and therefore accumulate translational preinitiation complexes. Three of the mutants exhibit a shortage of mature 25S rRNA, and one accumulates rRNA precursors. The accumulation of rRNA precursors suggests that ribosome assembly may be slowed in this mutant. These phenotypes lead us to propose that mutants containing the rpl16b alleles are defective for 60S subunit assembly rather than function. In the mutant carrying the rpl16b-1 allele, ribosomes initiate translation at the noncanonical codon AUA, at least on the rpl16b-1 mRNA, bringing to light a possible connection between the rate and the fidelity of translation initiation.

scholarly journals Amino acid substitutions enhancing thermostability of Bacillus polymyxa β-glucosidase A

1996 ◽  
Vol 314 (3) ◽  
pp. 833-838 ◽  
Author(s):  
Cristina LOPEZ-CAMACHO ◽  
Jesus SALGADO ◽  
Juan Luis LEQUERICA ◽  
Alejo MADARRO ◽  
Esteban BALLESTAR ◽  
...  
Keyword(s):  
Glycosyl Hydrolase ◽  
Gene Transformation ◽  
Amino Acid Substitutions ◽  
Bacillus Polymyxa ◽  
Cd Spectra ◽  
Wild Type ◽  
Wild Type Enzyme ◽  
Thermophilic Species ◽  
Hydroxylamine Mutagenesis ◽  
Α Helix

Mutations enhancing the thermostability of β-glucosidase A of Bacillus polymyxa, a family 1 glycosyl hydrolase, have been obtained after hydroxylamine mutagenesis of a plasmid containing the bglA gene, transformation of Escherichia coli with the mutagenized plasmid, and identification of transformant colonies that showed β-glucosidase activity after a thermal treatment that inactivated the wild-type enzyme. Two additive mutations have been characterized that cause replacement of glutamate at position 96 by lysine and of methionine at position 416 by isoleucine respectively. The thermoresistant mutant enzymes showed increased resistance to other denaturing agents, such as pH and urea, while their kinetic parameters did not change. CD spectra indicated that the E96K replacement caused an increase in α-helix content. The observed effect of the M416I mutation is consistent with the lower content of cysteine and methionine found in family 1 enzymes of thermophilic species compared with similar ones from mesophilic organisms.

Mechanism of hydroxylamine mutagenesis: Role of tautomerism, conformation and proton exchange on base pairing between the promutagen N6 methoxyadenosine and uridine

1993 ◽  
Vol 46 (3) ◽  
pp. 207-215 ◽  
Author(s):  
Borys Kierdaszuk ◽  
Charlotta Johansson ◽  
Torbjorn Drakenberg ◽  
Ryszard Stolarski ◽  
David Shugar
Keyword(s):  
Proton Exchange ◽  
Base Pairing ◽  
Hydroxylamine Mutagenesis
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