The Amino Acid Sequence of Cytochrome c from Debaryomyces kloeckeri*

Sugeno, Koichi; Narita, Kozo; Titani, Koiti

doi:10.1093/oxfordjournals.jbchem.a129681

Cited by 34 publications

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“…occidentalis, K. lactis, C. glabrata, Aspergillus nidulans and C. albicans, which were deduced from the corresponding DNA sequences, and the co-and post-translational modification of these proteins has not been directly determined. The sequences are from: S. cerevisiae, iso-1-cytochrome c (Iso-1: Narita and Titani, 1969;DeLange et al, 1970;Smith et al, 1979); S. cerevisiae, iso-2-cytochrome c (Iso-2; Montgomery et al, 1980); C. glabrata (Clark-Walker, 1991); H. anomala (Becam and Lederer, 1981); K. lactis (Freire-Picos et al, 1993); Debaryomyces kloeckeri (Sugeno et al, 1971); C. albicans (this investigation); Sch. occidentalis (Amegadzie et al, 1990); C. krusei (Narita and Titani, 1968;Delange et al, 1970;Lederer, 1972;Machleidt et al, 1973); A. nidulans (Raitt et al, 1994); A. niger (Chin et al, 1989); Neurospora crassa (Heller and Smith, 1966;Delange et al, 1969;Stuart et al, 1987); Humicola lanuginosa (Morgan et al, 1972); Ustilago sphaerogena (Bitar et al, 1972); Schizosaccharomyces pombe (Simon- Becam et al, 1978;Russell and Hall, 1982).…”

Section: Resultsmentioning

confidence: 99%

“…Many fungal cytochromes c contain N-trimethyllysine at the single position 72, including iso-1-cytochrome c and iso-2-cytochrome c (DeLange et al, 1970) from S. cerevisiae, and cytochromes c from N. crassa (DeLange et al, 1969), Debaromyces kloeckeri (Sugeno et al, 1971), Candida krusei (DeLange et al, 1970), but not from Ustilago sphaerogena (Bitar et al, 1972). Humicola lanuginosa cytochrome c contains N--trimethyllysine at position 86 and N-dimethyllysine at position 72 (Morgan et al, 1972).…”

Section: Resultsmentioning

confidence: 99%

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Phylogenetic Relationships of Fungal Cytochromesc

Janbon

Rustchenko

Klug

et al. 1997

Yeast

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The CYC1 gene encoding cytochrome c in the yeast Candida albicans was cloned by complementation of a cytochrome c‐deficient mutant of Saccharomyces cerevisiae, and its DNA sequence was determined. The analysis of the amino acid sequences of cytochrome c from 14 fungal species and two isoforms from S. cerevisiae revealed sequences unique to fungi, and revealed a phylogenetic relationship with a pronounced divergence between Schizosaccharomyces pombe and other ascomycetous budding yeast. The C. albicans CYC1 cytochrome c sequence has been assigned Accession Number U57896 in the GenBank/EMBL database. © 1997 John Wiley & Sons, Ltd.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Phylogenetic Relationships of Fungal Cytochromesc

Janbon

Rustchenko

Klug

et al. 1997

Yeast

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“…Histone H2B usually has a free amino-terminal residue, which is proline 111. However, in some histones H2B of plant or animal origin the amino-terminal end has been reported blocked by a group which remains unknown [l, 201. The postsynthetic methylation of the amino-terminal residue has already been observed in Escherichiu coli ribosomal proteins L11 [34], L16, L33 and S11 [35] and in Crithidiu oncopeIti cytochrome c [36]. N-dimethylproline is the blocked amino-terminal residue of the protozoan cytochrome c.…”

Section: Discussionmentioning

confidence: 99%

Primary structure of histone H2B from gonads of the starfish Asterias rubens

Martinage

Briand

et al. 1985

European Journal of Biochemistry

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The complete amino acid sequence (121 residues) of histone H2B from gonads of the starfish Asterias rubens has been established from structural data obtained essentially from large fragments generated by cleavage of histone H2B at aspartyl residues and by limited hydrolysis of the dimer H2A-H2B with mouse submaxillary gland protease.No real sequence homology can be found between the amino-terminal sequence (residues 1-21) of starfish and calf H2B. One non-conservative substitution (serine-32 in calf + lysine-28 in starfish) leads to the presence of a cluster of eight basic residues (sequence 23 -30) and to the disappearance of a potential site of phosphorylation.A particular structural feature of starfish histone H2B is the presence of N-dimethylproline at its aminoterminal end. By comparison with N-terminal acetylation, which is commonly found in histones, N-terminal methylation is rarely observed. At the present time the functional significance of the N-terminal methylation as well as that of the proline-rich nature of the amino-terminal sequence of the starfish histone H2B remain to be defined.The amino acid sequences of core particle histones were first determined for calf thymus, then in a variety of tissues and species [l] [21] and found to be located in the N-terminal region.The peculiar structural characteristics and the higher degree of variability observed in histone H2B from Echinidae [I] have led us to investigate the primary structure of histone H2B in Asterinidae, another family of the phylum echinoderms.In this paper we report the complete amino acid sequence of histone H2B from gonads of the starfish Asterias rubens. This sequence was established from structural data provided by tryptic peptides and large fragments derived from cleavage of the protein at aspartic acid and arginine residues.Starfish histone H2B is devoid of a free amino-terminal group. The blocking group has been identified as dimethylproline. The amino-terminal blocking of histones by methylation has only been observed previously in Tetrahymena histone H2B [22]. MATERIALS AND METHODS MaterialsMature starfish were obtained from the Station Marine, Wimereux (France). After excision, gonads were frozen in solid C 0 2 and kept at -20" C until use.Trypsin (treated with TosPheCH2C1) and carboxypeptidases A and B (treated with PhMeS0,F) were obtained from Worthington. Thermolysin was from Merck. Arg-C endoproteinase from mouse submaxillaris gland was purchased from Boehringer.Dimethylallylamine, propan-1 -01, dithioerythritol and anhydrous hydrazine were sequanal grade from Pierce. Benzene and chloro-1 -butane for sequential analysis were purchased from SDS (Peypin, France). Phenylisothiocyanate, heptane and heptafluorobutyric acid were sequanal grade from Merck. Polybrene was purchased from Aldrich and the dipeptide GlyGly from Sigma. All other reagents were of the highest purity available.Isolation of histone H2B and of histone dimer H2A-H2BChromatin was isolated from gonads as described in [23]. The crude fraction F2b was extracted...

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“…Many but not all fungi contain methylated lysine residues at one or two specific positions. Tml is found at the single position 72 in iso-1-cytochrome c and iso-2-cytochrome c (6) from Saccharomyces cerevisiae and cytochromes c from Neurospora crassa (1), Debaromyces kloeckeri (7), and Candida krusei (6) but not from Ustilago sphaerogena (8). Humicola languinosa cytochrome c contains N ⑀ -trimethyllysine at position 86 and N ⑀ -dimethyllysine at position 72 (9).…”

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confidence: 99%

Cytochrome c Methyltransferase, Ctm1p, of Yeast

Polevoda

Martzen

Das

et al. 2000

Journal of Biological Chemistry

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Cytochromes c from plants and fungi, but not higher animals, contain methylated lysine residues at specific positions, including for example, the trimethylated lysine at position 72 in iso-1-cytochrome c of the yeast Saccharomyces cerevisiae. Testing of 6,144 strains of S. cerevisiae, each overproducing a different open reading frame fused to glutathione S-transferase, previously revealed that YHR109w was associated with an activity that methylated horse cytochrome c. We show here that this open reading frame, denoted Ctm1p, is specifically responsible for trimethylating lysine 72 of iso-1-cytochrome c. Unmethylated forms of cytochrome c but not other proteins or nucleic acids are methylated in vitro by Ctm1p produced in S. cerevisiae or Escherichia coli. Iso-1-cytochrome c purified from a ctm1-⌬ strain is not trimethylated in vivo, whereas the K72R mutant form, or the trimethylated Lys-72 form of iso-1-cytochrome c, are not significantly methylated by Ctm1p in vitro. Like apocytochrome c, but in contrast to holocytochrome c, Ctm lp is located in the cytosol, consistent with the view that the natural substrate is apocytochrome c. The ctm1-⌬ strain lacking the methyltransferase did not exhibit any growth defect on a variety of media and growth conditions, and the unmethylated iso-1-cytochrome c was produced at the normal level and exhibited the normal activity in vivo. Ctm1p and cytochrome c were coordinately regulated during anaerobic to aerobic transition, a finding consistent with the view that this methyltransferase evolved to act on cytochrome c.

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The Amino Acid Sequence of Cytochrome c from Debaryomyces kloeckeri*

Cited by 34 publications

References 0 publications

Phylogenetic Relationships of Fungal Cytochromesc

Phylogenetic Relationships of Fungal Cytochromesc

Primary structure of histone H2B from gonads of the starfish Asterias rubens

Cytochrome c Methyltransferase, Ctm1p, of Yeast

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