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Structural protein PDB id
1uhm
Jmol
Contents
Protein chain
78 a.a. *
* Residue conservation analysis
PDB id:
1uhm
Name: Structural protein
Title: Solution structure of the globular domain of linker histone homolog hho1p from s. Cerevisiae
Structure: Histone h1. Chain: a. Fragment: globular domain. Synonym: histone hho1p. Engineered: yes
Source: Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Gene: hho1. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
NMR struc: 20 models
Authors: K.Ono,O.Kusano,S.Shimotakahara,M.Shimizu,T.Yamazaki, H.Shindo,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref: K.Ono et al. (2003). The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy. Nucleic Acids Res, 31, 7199-7207. PubMed id: 14654695 DOI: 10.1093/nar/gkg931
Date:
05-Jul-03     Release date:   16-Dec-03    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P53551  (H1_YEAST) -  Histone H1
Seq:
Struc: 		258 a.a.
78 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     nucleus   2 terms 
  Biological process     nucleosome assembly   1 term 
  Biochemical function     DNA binding     1 term  

 

 
DOI no: 10.1093/nar/gkg931 Nucleic Acids Res 31:7199-7207 (2003)
PubMed id: 14654695  
 
 
The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy.
K.Ono, O.Kusano, S.Shimotakahara, M.Shimizu, T.Yamazaki, H.Shindo.
 
  ABSTRACT  
 
Hho1p is assumed to serve as a linker histone in Saccharomyces cerevisiae and, notably, it possesses two putative globular domains, designated HD1 (residues 41-118) and HD2 (residues 171-252), that are homologous to histone H5 from chicken erythrocytes. We have determined the three-dimensional structure of globular domain HD1 with high precision by heteronuclear magnetic resonance spectroscopy. The structure had a winged helix-turn-helix motif composed of an alphabetaalphaalphabetabeta fold and closely resembled the structure of the globular domain of histone H5. Interestingly, the second globular domain, HD2, in Hho1p was unstructured under physiological conditions. Gel mobility assay demonstrated that Hho1p preferentially binds to supercoiled DNA over linearized DNA. Furthermore, NMR analysis of the complex of a deletion mutant protein (residues 1-118) of Hho1p with a linear DNA duplex revealed that four regions within the globular domain HD1 are involved in the DNA binding. The above results suggested that Hho1p possesses properties similar to those of linker histones in higher eukaryotes in terms of the structure and binding preference towards supercoiled DNA.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19282449 F.Cui, and V.B.Zhurkin (2009).
Distinctive sequence patterns in metazoan and yeast nucleosomes: implications for linker histone binding to AT-rich and methylated DNA.
  Nucleic Acids Res, 37, 2818-2829.  
19017647 Q.Yu, H.Kuzmiak, Y.Zou, L.Olsen, P.A.Defossez, and X.Bi (2009).
Saccharomyces cerevisiae linker histone Hho1p functionally interacts with core histone H4 and negatively regulates the establishment of transcriptionally silent chromatin.
  J Biol Chem, 284, 740-750.  
18687885 A.Levy, M.Eyal, G.Hershkovits, M.Salmon-Divon, M.Klutstein, and D.J.Katcoff (2008).
Yeast linker histone Hho1p is required for efficient RNA polymerase I processivity and transcriptional silencing at the ribosomal DNA.
  Proc Natl Acad Sci U S A, 105, 11703-11708.  
15255891 A.C.Harvey, and J.A.Downs (2004).
What functions do linker histones provide?
  Mol Microbiol, 53, 771-775.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.