Crystal structure of globular domain of histone H5 and its implications for nucleosome binding

By Venki Ramakrishnan, J. Finch, V. Graziano, P. Lee, R. Sweet. 1993

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

1. H. Feng
2. K. Zaret
3. Peter B. Becker
4. J. Bednar
5. M. S. Luijsterburg
6. I. Garcia-Saez
7. A. Flaus
8. S. Balaji

Citations in the corpus

• Structural Mechanisms of Nucleosome Recognition by Linker Histones (2015, background): “…between the globular domain and two DNA-binding proteins (CAP and HNF-3g), the a3 helix of the globular domain was predicted to bind to the major groove of DNA (Ramakrishnan et al., 1993), whereas in our structure, the a3 helix binds to the minor groove of DNA, in a way similar to core histones.”
• ACF catalyses chromatosome movements in chromatin fibres (2008, background): “…Biology Organization |All Rights Reserved 0261-4189/08 www.embojournal.org &2008 European Molecular Biology Organization The EMBO Journal VOL 27 | NO 6 | 2008 EMBO THE JOURNAL 817 which may be due to the presence of a third DNA-binding surface in H5 (Ramakrishnan et al, 1993; Fan et al, 2005).”
• Identification of multiple distinct Snf2 subfamilies with conserved structural motifs (2006, background): “The linker histone-related domain in human SHPRH corresponds to the globular winged helix structure of histone H1 (188) and transcription factor HNF3 (189,190).”
• The many faces of the helix-turn-helix domain: transcription regulation and beyond. (2005, background): “The eukaryotes display their own families of specific transcription factors, such as the Forkhead-histone H1 [25,26] and E2F-DP1 families [159], and the basal transcription factors, such as the TFIIF(Rap30)-TFIIIC-63K family [160] that show structurally similar wHTH domains, but lack specific sequen”
• Pioneer Transcription Factors Target Partial DNA Motifs on Nucleosomes to Initiate Reprogramming (2015, unknown): “, 1993), which is similar to that of linker histone (Ramakrishnan et al., 1993), allows the protein to bind its DNA motif exposed on a nucleosome and access to silent chromatin (Cirillo and Zaret, 1999; Cirillo et al.”
• Structure and Dynamics of a 197 bp Nucleosome in Complex with Linker Histone H1. (2017, background): “The linker histone globular domain adopts a winged-helix DNA-binding fold (Ramakrishnan et al., 1993).”
• Forkhead transcription factors: key players in development and metabolism. (2002, background): “A winged helix fold remarkably similar to that of forkhead proteins, except for the lack of a second wing, is found in the linker histones H1 and H5 (Brennan, 1993; Cerf et al., 1994; Clark et al., 1993; Ramakrishnan et al., 1993).”
• Pioneer transcription factors: establishing competence for gene expression. (2011, background): “The crystal structures of the DNA-binding domains of linker histone (Ramakrishnan et al. 1993) and FoxA3 (Clark et al.”
• The Major Architects of Chromatin: Architectural Proteins in Bacteria, Archaea and Eukaryotes (2008, background): “Analysis of H1 mutants in combination with molecular modeling using available atomic structures suggested that one of the DNA-binding surfaces interacts with the major groove about one helical turn away from the nucleosome dyad (Ramakrishnan et al., 1993; Luger et al., 1997; Brown et al., 2006).”