Presence of calmodulin-like calcium-binding protein in Bacillus cereus T spores

Shyu, Yuan‐Tay

doi:10.1016/0378-1097(89)90493-x

Cited by 5 publications

(6 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The calcium binding surface component(s) like a calciumbinding protein (30,32) may be mutationally altered or absent in lOLD mutant spores (2).…”

Section: Restoration By Calcium Of L-alanine-induced Germinabilities mentioning

confidence: 99%

“…In view of numerous reports that the germinability lost as a result of conversion to the H+ form spore could be restored upon calcium reloading (25)(26)(27)(28), the extent of loss of the coat component responsible for calcium binding during the SDS-DTT extraction appeared to be one of the critical factors affecting successful calcium loading for those spores. The calcium binding surface component(s) like a calciumbinding protein (30,32) may be mutationally altered or absent in lOLD mutant spores (2).…”

Section: Restoration By Calcium Of L-alanine-induced Germinabilities mentioning

confidence: 99%

See 1 more Smart Citation

Involvement of Calcium in Germination of Coat‐Modified Spores of Bacillus cereus T

Shibata

Miyoshi

Osato

et al. 1992

Microbiology and Immunology

View full text Add to dashboard Cite

The effect of calcium on germination of coat-modified Bacillus cereus T spores was investigated. Coat-modified spores produced either by chemical extraction (SDS-DTT-treated spores) or by mutagenesis (10LD mutant spores) were unable to germinate in response to inosine. While SDS-DTT-treated spores could germinate slowly in the presence of L-alanine, l OLD mutant spores could not germinate at all. The lost or reduced germinability of coat-modified spores was restored when exogenous Ca2+ was supplemented to the germination media. The calcium requirement of coat-modified spores for germination was fairly specific. The simultaneous presence of germinant with Ca2+ was also required for germination of coat-modified spores. The optimal recovery of germinability was obsei ved in the presence of 1.0 mm of calcium acetate. The calcium requirement itself was remarkably diminished under the condition in which L-alanine and a certain purine nucleoside analog, adenosine or inosine, coexisted. The lost or diminished germinability observed in SDS-DTT-treated spores or l OLD mutant spores may be attributed to the loss of calcium associated with the spore integuments.

show abstract

“…The calcium binding surface component(s) like a calciumbinding protein (30,32) may be mutationally altered or absent in lOLD mutant spores (2).…”

Section: Restoration By Calcium Of L-alanine-induced Germinabilities mentioning

confidence: 99%

Section: Restoration By Calcium Of L-alanine-induced Germinabilities mentioning

confidence: 99%

Involvement of Calcium in Germination of Coat‐Modified Spores of Bacillus cereus T

Shibata

Miyoshi

Osato

et al. 1992

Microbiology and Immunology

View full text Add to dashboard Cite

show abstract

“…CALP isolated from M. phlei reacted with anti-bovine brain calmodulin in double immunodi¡usion test and on Western blot. The pu-ri¢ed protein (obtained from immunoa¤nity column and on further resolution on C-18 RP-HPLC column) was able to activate cAMP phosphodiesterase and NAD kinase from pea seeds ( 32,33]. The UV spectrum of CALP from M. phlei showed maxima at 238 nm and 205 nm, indicating absence of tryptophan and tyrosine residues, respectively.…”

Section: Discussionmentioning

confidence: 99%

Isolation, purification and characterization of intracellular calmodulin like protein (CALP) from Mycobacterium phlei

Sarma¹

1998

FEMS Microbiology Letters

View full text Add to dashboard Cite

A monomeric acidic protein of 14 000 Da with an isoelectric point of 4.5 was isolated from Mycobacterium phlei, which stained poorly with Coomassie brilliant blue. This protein showed retardation in mobility in SDS-PAGE upon treatment with calcium, similar to eukaryotic calmodulin proteins. Activation of cAMP phosphodiesterase and NAD kinase by this protein was observed. The CD spectral analysis indicated that the CALP has 52% of L-conformation. The regular L-conformation of the calmodulin like protein was shifted to 46% K-helical structure when calcium ions reacted with the protein, however, 42% of the CALP still retained its original L-conformation. These observations indicated homology of this calcium binding protein with that of eukaryotic calmodulins in few structural and functional properties. z 1998 Federation of European Microbiological Societies. Published by Elsevier Science B.V.

show abstract

“…In E. coli, the average concentration of free intracellular calcium appears to be identical to that of higher organisms (10-7 M; Gangola and Rosen, 1987) and the level of total cytoplasmic calcium has been reported to increase substantially during division (Chang et al, 1986). In addition, proteins with calmodulin-like activities have been described in bacilli and in cyanobacteria (Fry et al, 1986(Fry et al, , 1991Shyu and Foegeding, 1989;Pettersen and Bergman, 1989) and a calmodulin-like gene has been sequenced from Streptomyces erythraeus (Swan et al, 1987). In recent years, many examples of regulation of protein activity in bacteria through changes in phosphorylation of specific amino acid residues have been described (Saier et al, 1990) including that of DnaK (Cegielska and Georgopoulos, 1989), a heat shock protein implicated in the initiation of DNA replication (Sakakibara, 1988).…”

Section: Introductionmentioning

confidence: 99%

A single base change in the acceptor stem of tRNA(3Leu) confers resistance upon Escherichia coli to the calmodulin inhibitor, 48/80.

et al. 1991

View full text Add to dashboard Cite

We have isolated several classes of spontaneous mutants resistant to the calmodulin inhibitor 48/80 which inhibits cell division in Escherichia coli K12. Several mutants were also temperature sensitive for growth and this property was exploited to clone a DNA fragment from an E. coli gene library restoring growth at 42 degrees C and drug sensitivity at 30 degrees C in one such mutant. Physical and genetic mapping confirmed that both the mutation and the cloned DNA were located at 15.5 min on the E. coli chromosome at a locus designated feeB. By subcloning, complementation analysis and sequencing, the feeB locus was identified as identical to the tRNA(CUALEU) gene. When the mutant locus was isolated and sequenced, the mutation was confirmed as a single base change, C to A, at position 77 in the acceptor stem of this rare Leu tRNA. In other studies we obtained evidence that this mutant tRNA, recognizing the rare Leu codon, CUA, was defective in translation at both permissive and non‐permissive temperatures. The feeB1 mutant is defective in division and shows a reduced growth rate at non‐permissive temperature. We discuss the possibility that the mutant tRNA(3Leu) is limiting for the synthesis of a polypeptide(s), requiring several CUA codons for translation which in turn regulates in some way the level or activity of the drug target, a putative cell cycle protein.

show abstract

Presence of calmodulin-like calcium-binding protein in Bacillus cereus T spores

Cited by 5 publications

References 8 publications

Involvement of Calcium in Germination of Coat‐Modified Spores of Bacillus cereus T

Involvement of Calcium in Germination of Coat‐Modified Spores of Bacillus cereus T

Isolation, purification and characterization of intracellular calmodulin like protein (CALP) from Mycobacterium phlei

A single base change in the acceptor stem of tRNA(3Leu) confers resistance upon Escherichia coli to the calmodulin inhibitor, 48/80.

Contact Info

Product

Resources

About