New twists on H2A.Z: a histone variant with a controversial structural and functional past.
Integration of histone variants into chromatin organization allows for functional specification of chromatin regions. Recent functional analyses of H2A.Z have ascribed to it a multiplicity of complex and often opposing roles in developmental and homeostatic regulation. However, although the manner in which this essential histone variant is able to mediate its effects is not entirely well understood, current work has sought to investigate its mode of action. It is becoming increasingly clear that H2A.Z does not necessarily act independently, but rather, in conjunction with trans-acting factors to elicit chromatin changes. The nature of these structural changes has remained somewhat controversial but nevertheless exemplifies the seemingly multifaceted nature of H2A.Z.
Department of Biochemistry and Microbiology, University of Victoria, BC, Canada.
Deanna
D
Dryhurst
Anita A
AA
Thambirajah
Juan
J
Ausió
D000595:Amino Acid Sequence; D000818:Animals; D002467:Cell Nucleus / Q000378:metabolism; D002843:Chromatin / Q000737:chemistry; D019281:Dimerization; D006570:Heterochromatin / Q000737:chemistry; D006657:Histones / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D047468:Immunoprecipitation; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000502:physiology; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000502:physiology*; D013329:Structure-Activity Relationship
D002843:Chromatin; D006570:Heterochromatin; D006657:Histones; C493530:Htz1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins