Calmodulin-like protein from Bacillussubtilis

Fry, Ilona J.; Villa, Leah; Kuehn, Glenn D.; Hageman, James H.

doi:10.1016/0006-291x(86)90549-8

Cited by 42 publications

(16 citation statements)

References 16 publications

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“…The Ca2+ requirement for growth in prokaryotes is not very well documented. Some evidence now exists for bacterial calmodulin-like proteins (Falah et al, 1988 ;Fry et al, 1986;Inouye et al, 1983;Swan et al, 1987Swan et al, , 1989, suggesting a regulatory function for Ca2+. On the other hand, Ca2+ circulation is described as an electrochemical process (for a review, see Rosen, 1987) associated with its export involving a Ca2+-ATPase in streptococci (Kobayashi et al, 1978;Ambudkar et al, 1986).…”

Section: Introductionmentioning

confidence: 99%

Calcium regulation of growth and differentiation in Streptococcus pneumoniae

Trombe

Clavé²,

Manias³

1992

Journal of General Microbiology

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Streptococcus pneumonk requires 0.15 mM-Ca2+ in the medium for optimal growth. Increasing the Ca2+ concentration to 1 mM triggers either a differentiathe state, competence for genetic transformation during exponential growth, or partial lysis as won as the cultures enter stationary phase. Genetic and physiological data both suggest that these responses are under the control of activator@), excreted in the presence of high Ca2+ concentrations. 45Ca2+ transport is also stimulated by the activator(s). The amiloride derivative 2',4-dimethylbenzarnil (DMB) inhibits 45Ca2+ transport and prevents lysis and competence development. This provides evidence in favour of the involvement of Ca2+ transport in competence and culture lysis. On the other hand, addition of DNA to a competent culture prevents lysis of wild-type bacteria while a mutant, defective for DNA uptake, is not protected from lysis by exogenous DNA. An hypothesis is proposed for competence induction as a global metabolic response to Ca2+, under the control of competence factor.

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Section: Introductionmentioning

confidence: 99%

Calcium regulation of growth and differentiation in Streptococcus pneumoniae

Trombe

Clavé²,

Manias³

1992

Journal of General Microbiology

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“…Schulman & Greengard, 1978), the wide ranging regulatory function of this Ca2+ binding protein first became apparent. Eventually renamed 'calmodulin', (Cheung et al, 1978), the protein rapidly became established as a 'ubiquitous' (Klee & Calmodulin is a heat stable, monomeric, globular protein and has, depending upon the eukaryotic source of the protein, a molecular mass ranging from 15-22 kDa (Burgess & Kretsinger, 1981;Fry et al, 1986). The monomer is encoded by a single gene which is considered to be highly conserved.…”

Section: Introductionmentioning

confidence: 99%

Calmodulin and calcium mediated regulation in prokaryotes

Onek

Smith

1992

Journal of General Microbiology

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“…While calmodulin was initially considered to be absent in bacteria (3, 6), calmodulin-like proteins (CAMLPs) exhibiting either calcium-binding properties or bovine phosphodiesterase (PDE)-stimulating properties were found in some bacteria (8,10,12,13,15,24,34,36) A917, 1993]. These results support the view that mycobacteria contain a protein functionally similar to eukaryotic calmodulin.…”

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confidence: 67%

Cloning and Expression of the Gene for a Novel Protein from Mycobacterium smegmatis with Functional Similarity to Eukaryotic Calmodulin

et al. 2003

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A calmodulin-like protein (CAMLP) from Mycobacterium smegmatis was purified to homogeneity and partially sequenced; these data were used to produce a full-length clone, whose DNA sequence contained a 55-amino-acid open reading frame. M. smegmatis CAMLP, expressed in Escherichia coli, exhibited properties characteristic of eukaryotic calmodulin: calcium-dependent stimulation of eukaryotic phosphodiesterase, which was inhibited by the calmodulin antagonist trifluoperazine, and reaction with anti-bovine brain calmodulin antibodies. Consistent with the presence of nine acidic amino acids (16%) in M. smegmatis CAMLP, there is one putative calcium-binding domain in this CAMLP, compared to four such domains for eukaryotic calmodulin, reflecting the smaller molecular size (approximately 6 kDa) of M. smegmatis CAMLP. Ultracentrifugation and mass spectral studies excluded the possibility that calcium promotes oligomerization of purified M. smegmatis CAMLP.Calmodulin, a highly conserved and ubiquitous protein in eukaryotic cells (16,17), is a small, heat-and acid-stable protein composed of about 155 amino acids; it undergoes a conformational change upon binding calcium and modulates the function of a number of target proteins (20,21,40). While calmodulin was initially considered to be absent in bacteria (3, 6), calmodulin-like proteins (CAMLPs) exhibiting either calcium-binding properties or bovine phosphodiesterase (PDE)-stimulating properties were found in some bacteria (8,10,12,13,15,24,34,36) A917, 1993]. These results support the view that mycobacteria contain a protein functionally similar to eukaryotic calmodulin. As part of our studies on a possible regulatory role of CAMLP in the growth and metabolism of mycobacteria, we report here the purification of CAMLP from M. smegmatis, the nucleotide sequence of the gene encoding CAMLP, and the expression and partial characterization of the protein.Purification of M. smegmatis CAMLP. The activity of M. smegmatis CAMLP was assayed by the method of Fry et al. (11) based on the stimulation of bovine heart PDE activity by eukaryotic calmodulin. M. smegmatis ATCC 14468 was grown from a stab in Brodie and Gray's medium (1.3% BactoCasamino Acids, 0.1% potassium fumarate, 0.2% Tween 80, 0.1% K 2 HPO 4 , 0.03% MgSO 4 , 0.002% FeSO 4 [pH 7.0], with KOH) (2) at 37°C in a rotary shaker for 2 to 3 days. With this used as a fresh inoculum, 12 1-liter cultures were grown overnight. The cells were sedimented at 10,000 ϫ g for 10 min at 4°C and washed with 10 mM Tris-HCl (pH 7.5). About 70 g (wet weight) of cells was obtained.All operations were carried out at 4°C except for the high-

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Calmodulin-like protein from Bacillussubtilis

Cited by 42 publications

References 16 publications

Calcium regulation of growth and differentiation in Streptococcus pneumoniae

Calcium regulation of growth and differentiation in Streptococcus pneumoniae

Calmodulin and calcium mediated regulation in prokaryotes

Cloning and Expression of the Gene for a Novel Protein from Mycobacterium smegmatis with Functional Similarity to Eukaryotic Calmodulin

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