Structure of the chromatin binding (chromo) domain from mouse modifier protein 1

Ball, Linda; Murzina, Natalia V.; Broadhurst, R. William; Raine, Andrew; Archer, Sharon J.; Stott, Francesca J.; Murzin, Alexey G.; Singh, Prim B.; Domaille, Peter J.; Laue, Ernest D.

doi:10.1093/emboj/16.9.2473

Cited by 170 publications

(173 citation statements)

References 70 publications

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“…Two-dimensional and three-dimensional NMR spectra for the resonance and NOE assignment were recorded essentially as described previously (23,24 (25,26). 15 N T 1 and T 2 relaxation rates were calculated by fitting decaying cross-peak intensities to single exponential decays using the program Sparky version 3.1 (T. D. Goddard and D. G. Kellner, University of California, San Francisco).…”

Section: Methodsmentioning

confidence: 99%

Solution Structure of Human Cofilin

Pope

Zierler-Gould

Kühne

et al. 2004

Journal of Biological Chemistry

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128

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Human actin-depolymerizing factor (ADF) and cofilin are pH-sensitive, actin-depolymerizing proteins. Although 72% identical in sequence, ADF has a much higher depolymerizing activity than cofilin at pH 8. To understand this, we solved the structure of human cofilin using nuclear magnetic resonance and compared it with human ADF. Important sequence differences between vertebrate ADF/cofilins were correlated with unique structural determinants in the F-actin-binding site to account for differences in biochemical activities of the two proteins. Cofilin has a short ␤-strand at the C terminus, not found in ADF, which packs against strands ␤3/␤4, changing the environment around Lys 96 , a residue essential for F-actin binding. A salt bridge involving His 133 and Asp 98 (Glu 98 in ADF) may explain the pH sensitivity of human cofilin and ADF; these two residues are fully conserved in vertebrate ADF/cofilins. Chemical shift perturbations identified residues that (i) differ in their chemical environments between wild type cofilin and mutants S3D, which has greatly reduced G-actin binding, and K96Q, which does not bind F-actin; (ii) are affected when G-actin binds cofilin; and (iii) are affected by pH change from 6 to 8. Many residues affected by G-actin binding also show perturbation in the mutants or in response to pH. Our evidence suggests the involvement of residues 133-138 of strand ␤5 in all of the activities examined. Because residues in ␤5 are perturbed by mutations that affect both G-actin and Factin binding, this strand forms a "boundary" or "bridge" between the proposed F-and G-actin-binding sites.

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Section: Methodsmentioning

confidence: 99%

Solution Structure of Human Cofilin

Pope

Zierler-Gould

Kühne

et al. 2004

Journal of Biological Chemistry

Self Cite

128

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“…The conserved carboxyl-terminal region, termed the chromo shadow domain (CSD), is related to the CD in primary amino acid sequence (25). Both the CD and the CSD have been the subject of extensive structural analysis (26)(27)(28)(29)(30). Each domain forms a hydrophobic pocket.…”

Section: Hp1 Follows Codementioning

confidence: 99%

Does heterochromatin protein 1 always follow code?

Kirschmann

Wallrath

2002

Proc. Natl. Acad. Sci. U.S.A.

170

175

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Heterochromatin protein 1 (HP1) is a conserved chromosomal protein that participates in chromatin packaging and gene silencing. A loss of HP1 leads to lethality in Drosophila and correlates with metastasis in human breast cancer cells. On Drosophila polytene chromosomes HP1 is localized to centric regions, telomeric regions, in a banded pattern along the fourth chromosome, and at many sites scattered throughout the euchromatic arms. Recently, one mechanism of HP1 chromosome association was revealed; the amino-terminal chromo domain of HP1 interacts with methylated lysine nine of histone H3, consistent with the histone code hypothesis. Compelling data support this mechanism of HP1 association at centric regions. Is this the only mechanism by which HP1 associates with chromosomes? Interest is now shifting toward the role of HP1 within euchromatic domains. Accumulating evidence in Drosophila and mammals suggests that HP1 associates with chromosomes through interactions with nonhistone chromosomal proteins at locations other than centric heterochromatin. Does HP1 play a similar role in chromatin packaging and gene regulation at these sites as it does in centric heterochromatin? Does HP1 associate with the same proteins at these sites as it does in centric heterochromatin? A first step toward answering these questions is the identification of sequences associated with HP1 within euchromatic domains. Such sequences are likely to include HP1 ''target genes'' whose discovery will aid in our understanding of HP1 lethality in Drosophila and metastasis of breast cancer cells.

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“…Fig. 2 shows the core structure of each CD present in cpSRP43, each derived using the homology building program Swiss model (31) and the coordinates from a determined threedimensional structure of a known chromatin binding domain from mouse modifier protein 1 (1AP0) (32). The models suggest that the most highly conserved residues found among the three predicted chromodomains likely stabilize the ␤-sheet structure.…”

Section: Domain Analysis Indicates the Presence Of Three Chromodomainmentioning

confidence: 99%

“…The height of each letter indicates the relative level of similarity at each position. B, the three CDs of cpSRP43 were modeled by using the homology building program Swiss model (31), and the coordinates are from an NMR structure of 1APO, a binding domain from mouse modifier protein 1 (32). Representations were generated using Pymol (Delano Scientific).…”

Section: Fig 2 Conserved Structural Features Of Cpsrp43 Cdsmentioning

confidence: 99%