Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs.

Hill, Caroline S.; Rimmer, J.M.; Green, B.N.; Finch, J.T.; Thomas, Jean O.

doi:10.1002/j.1460-2075.1991.tb07720.x

Cited by 112 publications

(58 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In our in vitro system consisting of only DNA, core histones, and highly phosphorylated linker histones obtained from mitotic cells, there was a distinct negative effect according to the formation of oligonucleosome aggregates, which was neutralized after removal of the phosphate groups with alkaline phosphatase. Our findings therefore support the idea that phosphorylation at mitosis relieves constraints due to loosening of protein-DNA interaction, thereby permitting mechanisms other than H1 histone phosphorylation to condense the chromatin (21).…”

Section: Discussionsupporting

confidence: 84%

“…Previous analysis of the structural role of H1 histones demonstrated that three subfractions of H1 histones differ in their effectiveness in condensing DNA fibers into ordered aggregates (17) and that histone subtype H1t, compared with other subtypes, differs in its ability to condense chromatin (18,19). Furthermore, differences in the binding of H1 variants to DNA or phosphorylated H1 histones to DNA have been shown (20,21).The present work was undertaken to extend these earlier binding studies using an in vitro assay developed by Wolffe and Hayes (22), enabling us to systematically study the binding of all known linker histones to a model chromatin complex. The complex is based on a DNA fragment containing the mouse mammary tumor virus long terminal repeat (MMTV LTR) 1 promotor, the chromatin structure of which has been well characterized (23).…”

mentioning

confidence: 98%

mentioning

confidence: 99%

See 2 more Smart Citations

In Vitro Binding of H1 Histone Subtypes to Nucleosomal Organized Mouse Mammary Tumor Virus Long Terminal Repeat Promotor

Talasz

Sapojnikova²,

Helliger

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

The binding of all known linker histones, named H1a through H1e, including H1 0 and H1t, to a model chromatin complex based on a DNA fragment containing the mouse mammary tumor virus long terminal repeat promotor was systematically studied. As for the histone subtype H1b, we found a dissociation constant of 8 -16 nM to a single mononucleosome (210 base pairs), whereas the binding constant of all other subtypes varied between 2 and 4 nM. Most of the H1 histones, namely H1a, H1c, H1d/e, and H1 0 , completely aggregate polynucleosomes (1.3 kilobase pairs, 6 nucleosomes) at 270 -360 nM, corresponding to a molar ratio of six to eight H1 molecules per reconstituted nucleosome. To form aggregates with the histones H1t and H1b, however, greater amounts of protein were required. Furthermore, our results show that specific types of in vivo phosphorylation of the linker histone tails influence both the binding to mononucleosomes and the aggregation of polynucleosomes. S phase-specific phosphorylation with one to three phosphate groups at specific sites in the C terminus influences neither the binding to a mononucleosome nor the aggregation of polynucleosomes. In contrast, highly phosphorylated H1 histones with four to five phosphate groups in the C and N termini reveal a very high binding affinity to a mononucleosome but a low chromatin aggregation capability. These findings suggest that specific S phase or mitotic phosphorylation sites act independently and have distinct functional roles.H1 histones are a heterogeneous group of at least five subtypes with closely related but nonetheless different primary structures (1, 2). Two further H1 subtypes are known: the histone H1 0 , which is found in nonreplicative tissues (3, 4) and in rapidly proliferating cells (5), and the testis-specific histone variant H1t (6). The various linker histones containing a globular central region flanked by highly basic and hydrophilic C-and N-terminal tails (7,8) bind to the nucleosome and promote the organization of nucleosomes to a higher order structure (9, 10).There is evidence that histone H1 may interact differently with transcriptionally active and inactive regions of chromatin (11). Linker histones are also thought to modulate nucleosome position (12, 13) and to influence replication efficiency in vitro (14).The presence of this large number of various H1 histone subtypes and their possible posttranslational modifications, such as phosphorylation (15), make it very probable that H1 histones play numerous structural and functional roles in chromatin. Until now, no specific role for the various variants has been established although Kaludov et al. (16) showed that the mouse histone H1b binds preferentially to a regulatory sequence within a mouse H3.2 replication-dependent histone gene. Previous analysis of the structural role of H1 histones demonstrated that three subfractions of H1 histones differ in their effectiveness in condensing DNA fibers into ordered aggregates (17) and that histone subtype H1t, compared with other subtypes, dif...

show abstract

Section: Discussionsupporting

confidence: 84%

mentioning

confidence: 98%

mentioning

confidence: 99%

See 1 more Smart Citation

In Vitro Binding of H1 Histone Subtypes to Nucleosomal Organized Mouse Mammary Tumor Virus Long Terminal Repeat Promotor

Talasz

Sapojnikova²,

Helliger

et al. 1998

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…These sperm histones are first expressed in spermatogonia and subsequently function as normal histones in transcription and replication during meiosis due to the fact that their basic N-terminal extensions are phosphorylated and thus neutralized (52). At the late spermatid stage, these N-terminal sequences become dephosphorylated (52) and subsequently stabilize the highly condensed and transcriptionally inert chromatin of the mature sperm by strong ionic interaction with linker DNA (30,36). In contrast, the CS histones constitute the chromatin of the transcriptionally active oocyte and egg (14,35) and participate as maternally stored proteins in chromatin remodeling of the male pronucleus in the zygote (55).…”

Section: Discussionmentioning

confidence: 99%

The Five Cleavage-Stage (CS) Histones of the Sea Urchin Are Encoded by a Maternally Expressed Family of Replacement Histone Genes: Functional Equivalence of the CS H1 and Frog H1M (B4) Proteins

Mandl

Brandt

Superti‐Furga

et al. 1997

Molecular and Cellular Biology

View full text Add to dashboard Cite

The cleavage-stage (CS) histones of the sea urchin are known to be maternally expressed in the egg, have been implicated in chromatin remodeling of the male pronucleus following fertilization, and are the only histone variants present in embryonic chromatin up to the four-cell stage. With the help of partial peptide sequence information, we have isolated and identified CS H1, H2A, H2B, H3, and H4 cDNAs from egg poly(A) ؉ mRNA of the sea urchin Psammechinus miliaris. All five CS proteins correspond to replacement histone variants which are encoded by replication-independent genes containing introns, poly(A) addition signals, and long nontranslated sequences. Transcripts of the CS histone genes could be detected only during oogenesis and in development up to the early blastula stage. The CS proteins, with the exception of H4, are unique histones which are distantly related in sequence to the early, late, and sperm histone subtypes of the sea urchin. In contrast, the CS H1 protein displays highest sequence homology with the H1M (B4) histone of Xenopus laevis. Both H1 proteins are replacement histone variants with very similar developmental expression profiles in their respective species, thus indicating that the frog H1M (B4) gene is a vertebrate homolog of the CS H1 gene. These data furthermore suggest that the CS histones are of ancient evolutionary origin and may perform similar conserved functions during oogenesis and early development in different species.Histones are basic proteins that associate with each other and nuclear DNA to form the nucleosome. This basic unit of chromatin consists of two molecules each of the core histones H2A, H2B, H3, and H4, while the H1 protein interacts both with the histone octamer and with linker DNA and is responsible for packaging nucleosomes into higher-order structures. The core histones H3 and H4 are almost invariant in evolution. The less well conserved H2A and H2B proteins often occur as different subtypes within the same organism, while the H1 protein is the most variable of all histones (reviewed in reference 66).The expression of the majority of histone genes is tightly coupled to DNA synthesis by specific transcriptional and posttranscriptional mechanisms. These so-called replication histone genes code for mRNAs with short 5Ј and 3Ј untranslated regions; they lack introns and polyadenylation sequences but instead end in a 3Ј-terminal palindrome (11, 34) that serves as a recognition sequence for U7 snRNP-mediated 3Ј processing of histone pre-mRNA (5). A minor group of histone genes is expressed at a basal level throughout the cell cycle in proliferating cells and at a reduced but significant rate in quiescent cells, where their proteins gradually replace the replicationdependent histones in the chromatin (73, 74). These so-called replacement histone genes contain introns, code for polyadenylated mRNA with long untranslated sequences, and are thus classical RNA polymerase II transcription units (9,22,68).The sea urchin genome contains four distinct histone gene familie...

show abstract

“…One of these peptides was derived from DNA binding proteins and contained the repeated SPKR motif, which is a substrate for CDKs. They found that a mitotic event indeed greatly improved expression efficiency with this peptide based pDNA carrier and asssumed that phosphorylation in the early phases of mitosis strongly diminished the carriers affinity towards pDNA and thus resulted in pDNA release at the time it has the best chances to enter the daughter nuclei [188]. An additional advantage is that the pDNA is well protected against nucleases in the cytosol until it has the possibility to be enclosed in the daughter nuclei [8].…”

Section: Cell-division Responsive Nanoparticlesmentioning

confidence: 99%

Intracellular partitioning of cell organelles and extraneous nanoparticles during mitosis

Symens

Soenen

Rejman

et al. 2012

Advanced Drug Delivery Reviews

View full text Add to dashboard Cite

Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs.

Cited by 112 publications

References 50 publications

In Vitro Binding of H1 Histone Subtypes to Nucleosomal Organized Mouse Mammary Tumor Virus Long Terminal Repeat Promotor

In Vitro Binding of H1 Histone Subtypes to Nucleosomal Organized Mouse Mammary Tumor Virus Long Terminal Repeat Promotor

The Five Cleavage-Stage (CS) Histones of the Sea Urchin Are Encoded by a Maternally Expressed Family of Replacement Histone Genes: Functional Equivalence of the CS H1 and Frog H1M (B4) Proteins

Intracellular partitioning of cell organelles and extraneous nanoparticles during mitosis

Contact Info

Product

Resources

About