Dataset Information

The methylated DNA binding protein-2-H1 (MDBP-2-H1) consists of histone H1 subtypes which are truncated at the C-terminus.

ABSTRACT: The methylated DNA binding protein-2-H1 (MDBP-2-H1), present in rooster liver, is a member of the histone H1 family which inhibits transcription by binding selectively to methylated promoters. Here we have determined the primary structure of MDBP-2-H1. A comparison between histone H1 and MDBP-2-H1 was achieved by analyzing reversed phase HPLC-purified and V8-digested proteins by mass spectrometry and/or microsequencing. In rooster liver the most abundant histone H1 subtypes are H1 01 and H1 11L. Similarly, MDBP-2-H1 contains the same subtypes of histone H1. The histone H1 subtype H1 01 in MDBP-2-H1 has 150 amino acids, whereas the full-size histone H1 01 is 218 amino acids. The difference in mass between the two proteins is explained by C-terminal truncation of histone H1 01.

SUBMITTER: Schwarz S

PROVIDER: S-EPMC147137 | biostudies-other | 1997 Dec

REPOSITORIES: biostudies-other

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The methylated DNA binding protein-2-H1 (MDBP-2-H1) consists of histone H1 subtypes which are truncated at the C-terminus.

Schwarz S S Hess D D Jost J P JP

Nucleic acids research 19971201 24

The methylated DNA binding protein-2-H1 (MDBP-2-H1), present in rooster liver, is a member of the histone H1 family which inhibits transcription by binding selectively to methylated promoters. Here we have determined the primary structure of MDBP-2-H1. A comparison between histone H1 and MDBP-2-H1 was achieved by analyzing reversed phase HPLC-purified and V8-digested proteins by mass spectrometry and/or microsequencing. In rooster liver the most abundant histone H1 subtypes are H1 01 and H1 11L. ...[more]

PMID: 9396815

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Project description:BackgroundHistone H1 is involved in the formation and maintenance of chromatin higher order structure. H1 has multiple isoforms; the subtypes differ in timing of expression, extent of phosphorylation and turnover rate. In vertebrates, the amino acid substitution rates differ among subtypes by almost one order of magnitude, suggesting that each subtype might have acquired a unique function. We have devised a competitive assay to estimate the relative binding affinities of histone H1 mammalian somatic subtypes H1a-e and H1 degrees for long chromatin fragments (30-35 nucleosomes) in physiological salt (0.14 M NaCl) at constant stoichiometry.ResultsThe H1 complement of native chromatin was perturbed by adding an additional amount of one of the subtypes. A certain amount of SAR (scaffold-associated region) DNA was present in the mixture to avoid precipitation of chromatin by excess H1. SAR DNA also provided a set of reference relative affinities, which were needed to estimate the relative affinities of the subtypes for chromatin from the distribution of the subtypes between the SAR and the chromatin. The amounts of chromatin, SAR and additional H1 were adjusted so as to keep the stoichiometry of perturbed chromatin similar to that of native chromatin. H1 molecules freely exchanged between the chromatin and SAR binding sites. In conditions of free exchange, H1a was the subtype of lowest affinity, H1b and H1c had intermediate affinities and H1d, H1e and H1 degrees the highest affinities. Subtype affinities for chromatin differed by up to 19-fold. The relative affinities of the subtypes for chromatin were equivalent to those estimated for a SAR DNA fragment and a pUC19 fragment of similar length. Avian H5 had an affinity ~12-fold higher than H1e for both DNA and chromatin.ConclusionH1 subtypes freely exchange in vitro between chromatin binding sites in physiological salt (0.14 M NaCl). The large differences in relative affinity of the H1 subtypes for chromatin suggest that differential affinity could be functionally relevant and thus contribute to the functional differentiation of the subtypes. The conservation of the relative affinities for SAR and non-SAR DNA, in spite of a strong preference for SAR sequences, indicates that differential affinity alone cannot be responsible for the heterogeneous distribution of some subtypes in cell nuclei.

Dataset Information

The methylated DNA binding protein-2-H1 (MDBP-2-H1) consists of histone H1 subtypes which are truncated at the C-terminus.

Publications

The methylated DNA binding protein-2-H1 (MDBP-2-H1) consists of histone H1 subtypes which are truncated at the C-terminus.

Similar Datasets

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