| General information | | DisProt: | DP00423 | | Name: | Histone H1 | | Synonym(s): | H1_YEAST
Hho1p
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P53551 | | UniGene: | | | SwissProt: | H1_YEAST | | TrEMBL: | | | NCBI (GI): | 1708096 | | Source organism: | Saccharomyces cerevisiae (Baker's yeast) | | Sequence length: | 258 | | Percent disordered: | 32% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MAPKKSTTKT TSKGKKPATS KGKEKSTSKA AIKKTTAKKE EASSKSYREL IIEGLTALKE - 60
RKGSSRPALK KFIKENYPIV GSASNFDLYF NNAIKKGVEA GDFEQPKGPA GAVKLAKKKS - 120
PEVKKEKEVS PKPKQAATSV SATASKAKAA STKLAPKKVV KKKSPTVTAK KASSPSSLTY - 180
KEMILKSMPQ LNDGKGSSRI VLKKYVKDTF SSKLKTSSNF DYLFNSAIKK CVENGELVQP - 240
KGPSGIIKLN KKKVKLST
|
| Functional narrative |
Nucleosomes are the structural units of chromatin for all eukaryotes, and consist of DNA wrapped around a histone octamer composed of core histones (H2A, H2B, H3 and H4). In addition to these core histones, linker histone H1 and its variants are known to associate with the linker region of DNA between nucleosome core particles. It is generally accepted that linker histones are involved in chromatin condensation as well as the maintenance of its higher order structure, and also serve as integral components of mechanisms that control gene expression. Hho1p is a linker histone required for nucleosome packaging at restricted sites; suppresses DNA repair involving homologous recombination; not required for telomeric silencing, basal transcriptional repression, or efficient sporulation. Hho1p inhibits DNA repair by homologous recombination,
suggesting that it may act as a linker histone with a novel role. Hho1p forms a stable ternary complex with a reconstituted core dinucleosome. Could act as an H1-type linker histone. Has been shown to bind DNA.
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | HD2 or GII domain | | Location: | 171 - 252 | | Length: | 82 | | Region sequence: |
KASSPSSLTYKEMILKSMPQLNDGKGSSRIVLKKYVKDTFSSKLKTSSNFDYLFNSAIKK
CVENGELVQPKGPSGIIKLNKK | | Modification type: | Fragment
Native
| | PDB: | 1USS:A, 1YQA:A | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-DNA binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV (pH: 7.2; 100 mM NaCl and 10 mM sodium phosphate; 2.0 mm path length; 25 microM protein; from 5 to 90°C at 5°C intervals)
- Nuclear magnetic resonance (NMR) (298 K; pH: 6.2; 10% D2O/90% H2O, 100 mM NaCl and 10 mM sodium phosphate; 1 mM protein)
| References:
- Ali T, Coles P, Stevens TJ, Stott K, Thomas JO. "Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p." J Mol Biol. 2004; 338(1): 139-48. PubMed: 15050829
- Ono K, Kusano O, Shimotakahara S, Shimizu M, Yamazaki T, Shindo H. "The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy." Nucleic Acids Res. 2003; 31(24): 7199-207. PubMed: 14654695
- Sanderson A, Stott K, Stevens TJ, Thomas JO. "Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p." J Mol Biol. 2005; 349(3): 608-20. PubMed: 15878177
| Comments:Hho1p, has two domains (GI and GII) that are similar in sequence to the globular domain of H1 (and variants such as H5). The GI domain, like the globular domains of H1 and H5 is stably folded at low ionic strength (10 mM sodium phosphate) and gives strong protection of chromatosome-length DNA (approximately 166 bp) during micrococcal nuclease digestion of chromatin. Interestingly, the second globular
domain, GII is unstructured under physiological conditions and gives weak chromatosome protection. However, at high concentrations of large tetrahedral anions (phosphate, sulphate, perchlorate), which might mimic the charge-screening effects of DNA phosphate groups, GII is folded.
|
| References |
- Downs JA, Kosmidou E, Morgan A, Jackson SP. "Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone." Mol Cell. 2003; 6(11): 1685-92. PubMed: 12820979
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
