๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Genetic mapping of a mutation in Escherichia coli leading to a temperature-sensitive RNase D

โœ Scribed by Zaniewski, Richard ;Deutscher, Murray R.


Publisher
Springer
Year
1982
Tongue
English
Weight
580 KB
Volume
185
Category
Article
ISSN
0026-8925

No coin nor oath required. For personal study only.

โœฆ Synopsis


In order to determine the metabolic role of RNase D in Escherichia coli, we have attempted to isolate strains deficient in this enzyme. One strain containing a temperature-sensitive RNase D was found among a heavily mutagenized stock of strain temperature-sensitive for growth. Genetic mapping of the mutation responsible for the altered RNAse D enabled us to define the rnd locus, at 39.5-40.0 min on the E. coli map, which apparently specifies the RNase D structural gene. Using a Tn10 insertion near the rnd locus, we constructed isogenic strains containing RNase D and Rnase II mutations, alone or in combination. Although the original mutant isolate displayed temperature-sensitive growth. no growth phenotype was associated with the rnd mutation in wild type background, possibly because a substantial amount of RNase D remained in cells grown at 45 degrees C. However, elucidation of the map position of the rnd locus should prove useful for the isolation of other mutant strains with lower levels of RNase D.


๐Ÿ“œ SIMILAR VOLUMES


Genetic mapping of a putative temperatur
โœ Abdul Jabbar, M. ;Jayaraman, R. ๐Ÿ“‚ Article ๐Ÿ“… 1978 ๐Ÿ› Springer ๐ŸŒ English โš– 531 KB

A putative temperature-sensitive transcription mutant described earlier (Jabbar and Jayaraman, 1976) has been genetically mapped. The locus maps at 38 min to the left of aroD. The mutation is recessive to the wild type and it affects a gene probably other than the genes coding for the alpha and beta

A mutation leading to the total lack of
โœ Chippaux, M. ;Giudici, D. ;Abou-Jaoudรฉ, A. ;Casse, F. ;Pascal, M. C. ๐Ÿ“‚ Article ๐Ÿ“… 1978 ๐Ÿ› Springer ๐ŸŒ English โš– 441 KB

Mutants of E. coli, completely devoid of nitrite reductase activity with glucose or formate as donor were studied. Biochemical analysis indicates that they are simultaneously affected in nitrate reductase, nitrite reductase, fumarate reductase and hydrogenase activities as well as in cytochrome C552

Intragenic suppression of the temperatur
โœ Dass, S. Balachandra ;Jayaraman, R. ๐Ÿ“‚ Article ๐Ÿ“… 1985 ๐Ÿ› Springer ๐ŸŒ English โš– 508 KB

Starting from a transcription-defective strain harbouring a temperature-sensitive mutation in the fit gene, a rifampicin-resistant, temperature-insensitive derivative has been isolated. Genetic analysis of this derivative demonstrated the presence of a second temperature-sensitive mutation in the sa

Suppressors of temperature-sensitive mut
โœ Nashimoto, Hiroko ;Miura, Akiko ;Saito, Haruo ;Uchida, Hisao ๐Ÿ“‚ Article ๐Ÿ“… 1985 ๐Ÿ› Springer ๐ŸŒ English โš– 859 KB

Temperature-sensitive (ts) mutations were isolated within a ribosomal protein gene (rpsL) of Escherichia coli K12. Mutations were mapped by complementation using various transducing phages and plasmids carrying the rpsL gene, having either a normal or a defective promoter for the rpsL operon. One of

Characterization of a mutation conferrin
โœ Estevenon, Anne-Marie ;Martin, Bernard ;Sicard, Nicole ๐Ÿ“‚ Article ๐Ÿ“… 1985 ๐Ÿ› Springer ๐ŸŒ English โš– 545 KB

The isolation and characterization of a new mutation conferring radiation sensitivity in Escherichia coli is described. This mutation is located close to the gene coding for deoxycytidine deaminase, in the chromosomal region of the gat operon. It is very sensitive to gamma rays and exhibits a decrea

Mutation to rifampicin resistance at the
โœ Lisitsyn, N. A. ;Sverdlov, E. D. ;Moiseyeva, E. P. ;Danilevskaya, O. N. ;Nikifor ๐Ÿ“‚ Article ๐Ÿ“… 1984 ๐Ÿ› Springer ๐ŸŒ English โš– 208 KB

The unusual recombinant plasmid pRC19 carrying the N-terminal fragment of the Escherichia coli RNA polymerase rpoB gene was found to specify high level rifampicin resistance of E. coli cells. Sequence analysis of this plasmid revealed one substitution only: transversion G----T, leading to amino acid