Literature DB >> 7279666

Effect of thyrotropin on 32P-labelled histones H1 and H3 in specific populations of nucleosomes in the thyroid.

E Cooper, R J Palmer, S W Spaulding.   

Abstract

Thyrotropin (TSH) increases the labeling of histones of H1 and H3 in thyroid slices incubated with 32Pi. We have prepared nuclei from control and TSH-treated thyroid slices, digested them with micrococcal nuclease, and extracted specific populations of nucleosomes by salt fractionation. Mononucleosomes, derived from the most nuclease-sensitive regions of chromatin, appeared to be selectively enriched in 32P-labeled H1 and H3. However, we were able to detect TSH enhancement of H1 and H3 labeling only in nucleosome multimers derived from less nuclease-sensitive chromatin. Recent studies have indicated that transcriptionally competent regions of chromatin may be more susceptible to micrococcal nuclease digestion than inactive regions. Our results therefore suggest that H1 and H3 may be actively phosphorylated in transcriptionally competent chromatin; however, they suggest either that hormone-dependent phosphorylation of H1 and/or H3 does not confer transcriptional competence, or that not all transcriptionally competent chromatin is nuclease sensitive.

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Year:  1981        PMID: 7279666      PMCID: PMC327359          DOI: 10.1093/nar/9.14.3389

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


  32 in total

1.  Histone Hl-DNA interaction. Influence of phosphorylation on the interaction of histone Hl with linear fragmented DNA.

Authors:  B O Glotov; L G Nikolaev; S N Kurochkin; E S Severin
Journal:  Nucleic Acids Res       Date:  1977-04       Impact factor: 16.971

2.  Thyrotropin stimulation of the phosphorylation of serine in the N-terminal of thyroid H1 histones.

Authors:  F Lamy; R Lecocq; J E Dumont
Journal:  Eur J Biochem       Date:  1977-03-01

3.  Removal of histone H1 exposes a fifty base pair DNA segment between nucleosomes.

Authors:  J P Whitlock; R T Simpson
Journal:  Biochemistry       Date:  1976-07-27       Impact factor: 3.162

4.  Altered conformational effects of phosphorylated lysine-rich histone (f-1) in f-1--deoxyribonucleic acid complexes. Circular dichroism and immunological studies.

Authors:  A J Adler; B Schaffhausen; T A Langan; G D Fasman
Journal:  Biochemistry       Date:  1971-03-02       Impact factor: 3.162

5.  Cleavage of structural proteins during the assembly of the head of bacteriophage T4.

Authors:  U K Laemmli
Journal:  Nature       Date:  1970-08-15       Impact factor: 49.962

6.  The fractionation of high-molecular-weight ribonucleic acid by polyacrylamide-gel electrophoresis.

Authors:  U E Loening
Journal:  Biochem J       Date:  1967-01       Impact factor: 3.857

7.  High resolution acrylamide gel electrophoresis of histones.

Authors:  S Panyim; R Chalkley
Journal:  Arch Biochem Biophys       Date:  1969-03       Impact factor: 4.013

8.  Action of micrococcal nuclease on chromatin and the location of histone H1.

Authors:  M Noll; R D Kornberg
Journal:  J Mol Biol       Date:  1977-01-25       Impact factor: 5.469

9.  Studies on the role and mode of operation of the very-lysine-rich histones in eukaryote chromatin. Effect of A and B site phosphorylation on the conformation and interaction of histone H1.

Authors:  H W Rattle; T A Langan; S E Danby; E M Bradbury
Journal:  Eur J Biochem       Date:  1977-12

10.  Histone content in relation to amount of heterochromatin and developmental stage in three species of Drosophila.

Authors:  P Holmgren; B Rasmuson; T Johansson; G Sundquist
Journal:  Chromosoma       Date:  1976-02-13       Impact factor: 4.316

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  3 in total

Review 1.  Nuclear protein kinases.

Authors:  H R Matthews; V D Huebner
Journal:  Mol Cell Biochem       Date:  1984       Impact factor: 3.396

2.  Genome-wide profiling of salt fractions maps physical properties of chromatin.

Authors:  Steven Henikoff; Jorja G Henikoff; Akiko Sakai; Gabriel B Loeb; Kami Ahmad
Journal:  Genome Res       Date:  2008-12-16       Impact factor: 9.043

3.  HMG (high-mobility-group)-14/17-like proteins in calf thyroid. Thyrotropin-dependent phosphorylation and comparison with calf thymus proteins.

Authors:  E Cooper; S W Spaulding
Journal:  Biochem J       Date:  1983-12-01       Impact factor: 3.857

  3 in total

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