Chicken erythrocyte histone H5

Briand, Gilbert; Kmiecik, Daniel; Sáutière, Pierre; Wouters, Danièle; Borie-Loy, O.; Biserte, G; Mazen, A.; Champagne, M.

doi:10.1016/0014-5793(80)80167-0

Cited by 134 publications

(40 citation statements)

References 16 publications

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“…The observation that H5-containing chromatin begins to fold at lower ionic strength than H1-containing chromatin [32 -341, suggests that H5, in contrast to H1, is perceptibly influencing the linker DNA even at low ionic strength. Sequcnces used to calculate the number of residucs were chicken FI1 [16], chicken H5 [17], Echinus esculentus sperm I11 [I I] (and C. S . Hill, unpublished; very similar to Purechinus ungulosus sperm H1 [18]).…”

Section: Dna Condensation and Bendability In Histone-dna Complexesmentioning

confidence: 99%

Differences in the binding of H1 variants to DNA

Clark

Thomas

1988

European Journal of Biochemistry

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A study of the complexes formed between short linear DNA and three H1 variants, a typical somatic HI, and the extreme variants H5, from chicken erythrocytes, and spHl from sea urchin sperm, has revealed differences between HI, H5 and spHl that have implications for chromatin structure and folding.1. All three histones bind cooperatively to DNA in 35 mM NaCl forming similar, but not identical, rod-like complexes. With sufficiently long DNA the complexes may be circular, circles forming more easily with H5 and spH1 than with H1.2. The binding of H5 and spHl to DNA is cooperative even in 5 mM NaC1, resulting in well-defined thin filaments that appear to contain two DNA molecules bridged by histone molecules. In contrast, H1 binds distributively over all the DNA molecules in 5 mM NaCl, but forms short stretches similar in appearance to the thin filaments formed with H5 and spH1. Rods appear to arise from the intertwining of regular thin filaments containing cooperatively bound histone molecules on raising the NaCl concentration to 35 mM.3. The compositions of the rods correspond to one histone molecule for about every 47 bp (Hl), 81 bp (H5) and 112 bp (spHl), suggesting average spacings of 24 bp (Hl), 41 bp (H5) and 56 bp (spH1) in the component thin (double) filaments. Strikinaly, these values are proportional to the linker lengths of the chromatins in which Histone the particular H1 variant is themain or sole H1.H1 serves the dual function of sealing the two turns of DNA around the histone octamer in the nucleosome and of mediating the ordered, salt-dependent folding of the 10-nm filament to form the 30-nm filament in vitro [I]. Different H1 variants may occur in different species, cell types and developmental stages [2] (and references therein). The structural significance of these variants is poorly understood [2], but it seems likely that they may be involved in the generation of folded filaments of different stabilities (cf.[3]), and that they may thereby play a role in regulating the accessibility of genes for transcription. Since all current models for the higher-order structure of chromatin [4] (and references therein) envisage the interaction of H1 to be primarily with DNA rather than with the core histones, we have asked whether there are differences in the interaction of different H1 variants with DNA that might account for the different properties in v i m and in vivo of the chromatins in which a particular variant is the sole, or major, HI.In an extension of earlier work on H1-DNA complexes [5], we have made a systematic study of the histone-DNA complexes formed by three quite distinct members of the H1 family: a typical somatic H1 (chicken Hl); the extreme variant, H5, which is the major lysine-rich histone in terminally repressed mature-chicken erythrocytes [6] ; and another extreme variant, spH1, from repressed sea-urchin sperm [7]. Chicken-erythrocyte chromatin and particularly sea-urchin-sperm chromatin are both highly condensed, and in addition to their distinctive H1 histones have long nucleosom...

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Section: Dna Condensation and Bendability In Histone-dna Complexesmentioning

confidence: 99%

Differences in the binding of H1 variants to DNA

Clark

Thomas

1988

European Journal of Biochemistry

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“…non-coding strand). The fragment of cDNA cloned is 259 base pairs long and has an open reading frame, following the only AUG triplet, which corresponds to the codons for up to residue 46 of the H5 variant containing an arginyl residue at position 15 (40,41). In addition, it contains 118 nucleotides from the 5' non-translated region.…”

Section: Resultsmentioning

confidence: 99%

“…The sequence upstream of the ATG initiation codon is numbered with negative digits. The amino acid sequence deduced from the DNA sequence indicates that the cloned DNA corresponds to a fragment of the mRNA coding for the Arg (position 15) variant of histone H5 (41). The main types of direct repeats are indicated by bars over or underlining the nucleotide sequence, and by boxes.…”

Section: Agc Cgcggc Ggc Tcc Tcg (C)mentioning

confidence: 99%

Construction of chimeric plasmids containing histone H5 cDNA from hen erythrocyte. DNA sequence of a fragment derived from the 5′ region of H5 mRNA

Ruiz‐Vázquez

Ruiz-Carrillo

1982

Nucl Acids Res

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We report the construction and characterization of chicken erythrocyte histone H5 cDNA recombinant plasmids. cDNA was synthesized from poly(A)+ polysomal RNA enriched in H5 mRNA and inserted into the PseI site of pBR322. Several clones containing H5 cDNA sequences were obtained and one of them (p541), expressing H5 antigenic determinants, was sequenced. The DNA insert of p541 contains 118 nucleotides from the 5' non-translated region of H5 mRNA and sequences coding for up to residue 46 of the N-terminus of the arginine (position 15) H5 variant. There is a strikingly high number of repeated sequences both in the leader and coding region; among these, the octanucleotide 5' GCGGCG GC3' is found five times along the sequence. Although the H5 mRNA 5' leader is GC-rich (66%), there is an AT-rich region, about 16 nucleotides long, which shares strong homology with the leaders of sea urchin histone Hi mRNAs.

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“…Structural studies of the phosphorylated tryptic peptides isolated by ion-exchange chromatography on Chromobeads P (Technicon Corp.) allowed us to locate the phosphoserine residues in the sequence of the protein [13].…”

Section: Resultsmentioning

confidence: 99%

“…The recognition of such sequences by the cAMPindependent kinase from mouse plasmocytoma cells explains the narrow specificity of this kinase for the phosphorylation of histone H1 and of histone H5 which is closely related to histone H1 [13]. These sequences are only encountered in histones H 1 and H5 but not in core histones H2A, H2B, H3 and H4.…”

Section: Resultsmentioning

confidence: 99%