The amino acid sequence of the Tetrahymena calmodulin which specifically interacts with guanylate cyclase

Yazawa, Michio; Yagi, Koichi; Toda, Hiroko; Kondo, Kiyoshi; Narita, Kozo; Yamazaki, Reiko; Sobue, Kenji; Kakiuchi, Shiro; Nagao, Seiji; Nozawa, Yoshinori

doi:10.1016/0006-291x(81)90725-7

Cited by 114 publications

(31 citation statements)

References 20 publications

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“…Vertical arrows point to-in "Materials and Methods." Peak 1 is R1T3 (residues 31-37), peak 2 is wards amino termini of trypsin peptides obtained from subdigests of R1T2 (residues [14][15][16][17][18][19][20][21][22][23][24][25][26][27][28][29][30], and peak 3 is RITI (residues 1-13). Composiarginine peptides R I and R5.…”

Section: Resultsmentioning

confidence: 99%

“…Complete amino acid sequences have been determined for bovine brain (12,27,29) and human brain calmodulin (21). Nearly complete sequences have been published for rabbit skeletal muscle (6), bovine uterus (6), rat testis (4), sea anenome (24), Renilla (10), Tetrahymena (30), and scallop (25) calmodulins. In addition, protein sequences of the electric eel (15) and chicken (19) General.…”

Section: Methodsmentioning

confidence: 99%

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Structural Characterization of a Higher Plant Calmodulin

Lukas

Iverson²,

Schleicher³

et al. 1984

Plant Physiol.

107

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ABSTRACICalmodulin is a eukaryotic calcium binding protein which has several calcium-dependent in vitro activities. Presented in this report is a structural characterization of calmodulin from spinach leaves (Spinacia okracea determine what differences might exist in the primary structure of the plant protein compared to other known calmodulins. Any functional differences must be related to the covalent structure which, in turn, determines the three-dimensional structure. Presented here is amino acid sequence data and homologous alignments which provide a proposed primary structure of spinach calmodulin. Certain portions of the amino acid sequence of spinach calmodulin have appeared elsewhere (3, 27). MATERIALS AND METHODSCalmodulin is a eukaryotic Ca binding protein which modulates the activity of a number ofenzymes in vitro (13). Complete amino acid sequences have been determined for bovine brain (12,27,29) and human brain calmodulin (21). Nearly complete sequences have been published for rabbit skeletal muscle (6), bovine uterus (6), rat testis (4), sea anenome (24), Renilla (10), Tetrahymena (30), and scallop (25)

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Structural Characterization of a Higher Plant Calmodulin

Lukas

Iverson²,

Schleicher³

et al. 1984

Plant Physiol.

107

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“…The amino acid sequences of several calmodulins such as those from bovine brain [32], Renilla reniformis [39], Tetrahymena [31], and spinach [40] have been reported. The amino acid sequence of bovine calmodulin differs from that of calmodulin of the invertebrate R. reniformis in only seven positions.…”

Section: Discussionmentioning

confidence: 99%

Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae

et al. 1987

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Calmodulin from the yeast Saccharomyces cerevisiae was purified to complete homogeneity by hydrophobic interaction chromatography and HPLC gel filtration. The biochemical properties of the purified protein as calmodulin were examined under various criteria and its similarity and dissimilarity to other calmodulins have been described. Like other calmodulins, yeast calmodulin activated bovine phosphodiesterase and pea NAD kinase in a Ca2+-dependent manner, but its concentration for half-maximal activation was 8 -10 times that of bovine calmodulin. The amino acid composition of yeast calmodulin was different from those of calmodulins from other lower eukaryotes in that it contained no tyrosine, but more leucine and had a high ratio of serine to threonine. Yeast calmodulin did not contain tryptophanyl or tyrosyl residues, so its ultraviolet spectrum reflected the absorbance of phenylalanyl residues, and had a molar absorption coefficient at 259 nm of 1900 M-' cm-'. Ca2+ ions changed the secondary structure of yeast calmodulin, causing a 3% decrease in the ci-helical content, unlike its effect on other calmodulins. Antibody against yeast calmodulin did not cross-react with bovine calmodulin, and antibody against bovine calmodulin did not cross-react with yeast calmodulin, presumably due to differences in the amino acid sequences of the antigenic sites. It is concluded that the molecular structure of yeast calmodulin differs from those of calmodulins from other sources, but that its Ca2 +-dependent regulatory functions are highly conserved and essentially similar to those of calmodulins of higher eukaryotes.

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“…T2 (14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30) and T3 (31 -37) were sequenced directly up to their C-termini. T4 (38-72) was determined up to the 55th residue; trypsin cleaved the Met72 -Ser73 bond unusually.…”

Section: Sequence Determination Of the Tryptic Peptidesmentioning

confidence: 99%

“…T9 (91 -106) was identified up to the 96th residue [20]. Tetrahymena [21], Parumecium [22], wheat gcrm [I 21, and spinach [23] are aligncd in their four domain structures and numbered on the basis of that of human calmodulin. Substituted amino acid residues compared with human calmodulin arc shown and identical rcsidues are shown by dashes.…”

Section: Sequence Determination Of the Tryptic Peptidesmentioning

confidence: 99%

Amino acid sequence of calmodulin from Euglena gracilis

Toda

Yazawa

Yagi

1992

European Journal of Biochemistry

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The complete amino acid sequence of calmodulin from Euglena gracilis was determined by isolation and sequence analyses of peptides derived from calmodulin by digestion with trypsin and Stuphylococcus aureus V8 protease. Euglena calmodulin consists of 148 amino acid residues; it lacks tryptophan and cysteine and contains one tyrosine, three histidine and two N"-trimethyllysine residues/ molecule of the protein. Its N-terminus was blocked with an acetyl group and C-terminal lysine was trimethylated. Euglenu calmodulin is the first calmodulin so far examined in which the C-terminal lysine is trimethylated. [12], and eel, salmon, sea cucumber and fungi (unpublished).We report here the amino acid sequence of Euglena calmodulin and discuss amino acid substitutions. Materials and Methods, Figs S1 -S5 and Tables S1 and S2 appear as a Supplement at the end of this paper. RESULTS AND DISCUSSIONIsolation of tryptic peptides Tryptic peptides derived from Euglena calmodulin were separated by HPLC on a Cosmosil 5ClsP-30O column ( Note. The novcl amino acid sequencc data publishcd hcre have been deposited with the EMBL sequence data bank and are availablc Sl). Heterogeneous peptide fractions such as T7/T6-7/T12 and Tl/T2/T9/Tll were further purified by rechromatography on the same column using different solvent system as described above (Fig. S2). The 12 tryptic peptides were isolated. Amino acid compositions and overall yields of the purified tryptic peptides and whole Euglena calmodulin are listed in Table S1.Isolation of peptides generated by S. aureus V8 protease digestion S. aureus V8 protease peptides were separated in the same manner as for tryptic peptides. Heterogeneous peptide fractions were rechromatographed on a CIS column using a linear gradient of solvent B in solvent A as described in the text for separation of tryptic peptides ( Figs S3 and S4). The 15 peptides were isolated. Amino acid compositions and overall yields of the purificd peptides are listed in Table S2. N-terminal sequence analysisPeptide TI (1 -13) was resistant to Edman degradation, showing the absence of a free ainino-terminal group. TI was treated with acylamino-acid-releasing enzyme (AARE) prior to Edman degradation. Aliquots of the digest were subjected to automated Edman degradation and the remaining digests were scparated by HPLC on a CIS column (Fig. S5 and Fig. 1). The N-terminal acetylated amino acid was identified as alanine (0.8 mol/mol peptide) by amino acid analysis of fraction A1 after hydrolysis. The N-terminal acetyl group was also confirmed by FAB-MS analysis [I71 of the tryptic peptide, TI (1 -13) (data not shown). On the digestion of TI with acylamino-acid-releasing enzyme, minor cleavage of the Thr5 -His6 bond was observed due to intrinsic endopeptidase action of this enzyme. The results of sequence analysis of under accession number P11118.peptide TI are summarized in Fig. 1

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The amino acid sequence of the Tetrahymena calmodulin which specifically interacts with guanylate cyclase

Cited by 114 publications

References 20 publications

Structural Characterization of a Higher Plant Calmodulin

Structural Characterization of a Higher Plant Calmodulin

Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae

Amino acid sequence of calmodulin from Euglena gracilis

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