N-Trimethylalanine, a Novel Blocked N-Terminal Residue of Tetrahymena Histone H2B1

Nomoto, Minoru; Kyōgoku, Yoshimasa; Iwai, Koichi

doi:10.1093/oxfordjournals.jbchem.a134096

Cited by 35 publications

(22 citation statements)

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“…These studies have identified several modification sites but provided no information about the global state of the protein in terms of posttranslational modifications and relative stoichiometries of such modifications. The only previously published modification of Tetrahymena histone H2B is trimethylation of the N-terminal alanine residue (22). While our results confirmed this assignment, they have also established in addition that the protein's N-terminal alanine occurs free and with heterogeneous occurrence of mono-and dimethyl populations as well as the trimethyl reported much earlier (22).…”

Section: Discussionsupporting

confidence: 88%

“…Some fragments are common to both peptides. to reveal evidence for the most abundant form of the suite of modified proteins established much earlier (22). On this matter, we anticipated that digestion by the endoproteinase AspN would provide this information, but unfortunately none of the CID spectra acquired provided the conclusive evidence necessary for exact site assignments due to the presence of internal fragment ions isobaric with the expected discriminatory b ions sought in carrying out this digest.…”

Section: Discussionmentioning

confidence: 97%

“…Histone H2B is expressed as two closely related proteins H2B.1 and H2B.2, differing by only three amino acids (21). The only posttranslational modification reported about the Tetrahymena proteins is the trimethylation of their N-terminal alanine (22). However, the bovine histone H2B is reportedly acetylated at Lys-5, -12, -15, and -20 as well as ubiquitinated at Lys-120.…”

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confidence: 99%

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Characterization of Tetrahymena Histone H2B Variants and Posttranslational Populations by Electron Capture Dissociation (ECD) Fourier Transform Ion Cyclotron Mass Spectrometry (FT-ICR MS)

Medzihradszky

Zhang

Chalkley

et al. 2004

Molecular & Cellular Proteomics

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This work describes the nature and sequence information content of the electron capture dissociation mass spectra for the intact Tetrahymena histone H2B. Two major variants of this protein were present bearing nominal modifications of both ؉42 and ؉84 Da. This work describes identification of the nature of these two modifications. For example, using gas-phase selection and isolation of the ؉42-Da modified species, from a background of two H2B variants each present in six or more posttranslationally modified isoforms, we were able to determine that this ؉42-Da modification isoform bears trimethylation rather than acetylation. LC-CIDMS analysis was also employed on digested preparations to obtain complementary detail of the nature of site-specific posttranslational modifications. This study establishes that integration of the information from these two datasets provides a comprehensive map of posttranslational occupancy for each particular covalent assemblage selected for structural investigation. Molecular & Cellular Proteomics 3: 872-886, 2004.

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Section: Discussionsupporting

confidence: 88%

Section: Discussionmentioning

confidence: 97%

mentioning

confidence: 99%

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Characterization of Tetrahymena Histone H2B Variants and Posttranslational Populations by Electron Capture Dissociation (ECD) Fourier Transform Ion Cyclotron Mass Spectrometry (FT-ICR MS)

Medzihradszky

Zhang

Chalkley

et al. 2004

Molecular & Cellular Proteomics

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“…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]. …”

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confidence: 75%

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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“…In addition to histone lysine/arginine side chain methylation, methylation can also occur at the histone α-N terminus. For instance, methylations on the N terminus of histone H2B have been reported in Tetrahymena (Nomoto et al 1982), Arabidopsis thaliana (Bergmueller et al 2007), Drosophila melanogaster (Desrosiers and Tanguay 1988), and other invertebrates (Webb et al 2010). Recently, the N terminus of CENP-A, a centromere-specific histone H3 variant, was shown to be trimethylated by NRMT1, an α-N-methyltransferase.…”

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confidence: 99%

Molecular basis for histone N-terminal methylation by NRMT1

Yue

Zheng³

et al. 2015

Genes Dev.

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NRMT1 is an N-terminal methyltransferase that methylates histone CENP-A as well as nonhistone substrates. Here, we report the crystal structure of human NRMT1 bound to CENP-A peptide at 1.3 Å. NRMT1 adopts a core methyltransferase fold that resembles DOT1L and PRMT but not SET domain family histone methyltransferases. Key substrate recognition and catalytic residues were identified by mutagenesis studies. Histone peptide profiling revealed that human NRMT1 is highly selective to human CENP-A and fruit fly H2B, which share a common "X aaPro-Lys/Arg" motif. These results, along with a 1.5 Å costructure of human NRMT1 bound to the fruit fly H2B peptide, underscore the importance of the NRMT1 recognition motif.

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N-Trimethylalanine, a Novel Blocked N-Terminal Residue of Tetrahymena Histone H2B1

Cited by 35 publications

References 0 publications

Characterization of Tetrahymena Histone H2B Variants and Posttranslational Populations by Electron Capture Dissociation (ECD) Fourier Transform Ion Cyclotron Mass Spectrometry (FT-ICR MS)

Characterization of Tetrahymena Histone H2B Variants and Posttranslational Populations by Electron Capture Dissociation (ECD) Fourier Transform Ion Cyclotron Mass Spectrometry (FT-ICR MS)

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

Molecular basis for histone N-terminal methylation by NRMT1

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