scholarly journals 3P-199 Isolation of temperature sensitive mutants of the mechanosensitive channel MscL in Escherichia coli(The 46th Annual Meeting of the Biophysical Society of Japan)

2008 ◽  
Vol 48 (supplement) ◽  
pp. S158
Author(s):  
Kenjiro Yoshimura ◽  
Noriko Kasai
Keyword(s):  
Escherichia Coli ◽  
Annual Meeting ◽  
Mechanosensitive Channel ◽  
Temperature Sensitive ◽  
Temperature Sensitive Mutants ◽  
Biophysical Society

Temperature-sensitive mutants of MscL mechanosensitive channel

2019 ◽  
Vol 166 (3) ◽  
pp. 281-288 ◽  
Author(s):  
Naoto Owada ◽  
Megumi Yoshida ◽  
Kohei Morita ◽  
Kenjiro Yoshimura
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Structural Change ◽  
Cell Growth ◽  
Thermodynamic Stability ◽  
Transmembrane Helix ◽  
Mechanosensitive Channel ◽  
Temperature Sensitive ◽  
Temperature Sensitive Mutants ◽  
Membrane Stretching

Abstract MscL is a mechanosensitive channel that undergoes a global conformational change upon application of membrane stretching. To elucidate how the structural stability and flexibility occur, we isolated temperature-sensitive (Ts) mutants of Escherichia coli MscL that allowed cell growth at 32°C but not at 42°C. Two Ts mutants, L86P and D127V, were identified. The L86P mutation occurred in the second transmembrane helix, TM2. Substitution of residues neighbouring L86 with proline also led to a Ts mutation, but the substitution of L86 with other amino acids did not result in a Ts phenotype, indicating that the Ts phenotype was due to a structural change of TM2 helix by the introduction of a proline residue. The D127V mutation was localized in the electrostatic belt of the bundle of cytoplasmic helices, indicating that stability of the pentameric bundle of the cytoplasmic helix affects MscL structure. Together, this study described a novel class of MscL mutations that were correlated with the thermodynamic stability of the MscL structure.

scholarly journals LOCALIZED MUTAGENESIS FOR THE ISOLATION OF TEMPERATURE-SENSITIVE MUTANTS OF ESCHERICHIA COLI AFFECTED IN PROTEIN SYNTHESIS

Genetics ◽  
1979 ◽  
Vol 91 (2) ◽  
pp. 215-227
Author(s):  
W Scott Champney
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Temperature Sensitive ◽  
Chromosomal Locus ◽  
Ribosomal Subunits ◽  
Prolonged Incubation ◽  
Temperature Sensitive Mutants ◽  
Inhibition Of Growth ◽  
Localized Mutagenesis

ABSTRACT Two variations of the method of localized mutagenesis were used to introduce mutations into the 72 min region of the Escherichia coli chromosome. Twenty temperature-sensitive mutants, with linkage to markers in this region, have been examined. Each strain showed an inhibition of growth in liquid medium at 44°, and 19 of the mutants lost viability upon prolonged incubation at this temperature. A reduction in the rate of in vivo RNA and protein synthesis was observed for each mutant at 44°, relative to a control strain. Eleven of the mutants were altered in growth sensitivity or resistance to one or more of three ribosomal antibiotics. The incomplete assembly of ribosomal subunits was detected in nine strains grown at 44°. The characteristics of these mutants suggest that many of them are altered in genes for translational or transcriptional components, consistent with the clustering of these genes at this chromosomal locus.

scholarly journals 3P-205 Functional Reconstitution of salinarum Halorhodopsin Expressed in Escherichia coli(Photobiology:Vision & Photoreception,The 47th Annual Meeting of the Biophysical Society of Japan)

2009 ◽  
Vol 49 (supplement) ◽  
pp. S185
Author(s):  
Yasutaka Yamashita ◽  
Takashi Kikukawa ◽  
Masakatsu Kamiya ◽  
Tomoyasu Aizawa ◽  
Keiichi Kawano ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Annual Meeting ◽  
Biophysical Society

scholarly journals 3P206 Localization mechanism of the histidine kinase TorS of Escherichia coli controlling anaerobic respiration(Cell biology,The 48th Annual Meeting of the Biophysical Society of Japan)

2010 ◽  
Vol 50 (supplement2) ◽  
pp. S181
Author(s):  
Akiko Yamakawa ◽  
Hiroyuki Sawaki ◽  
Satomi Banno ◽  
Masayuki Yoshimoto ◽  
Takehiko Inaba ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Annual Meeting ◽  
Histidine Kinase ◽  
Cell Biology ◽  
Anaerobic Respiration ◽  
Biophysical Society
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