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Feng Wang Geng Li Mohammed Altaf Chenning Lu Mark A. Currie Aaron Johnson Danesh Moazed 《Proceedings of the National Academy of Sciences of the United States of America》2013,110(21):8495-8500
The regulated binding of effector proteins to the nucleosome plays a central role in the activation and silencing of eukaryotic genes. How this binding changes the properties of chromatin to mediate gene activation or silencing is not fully understood. Here we provide evidence that association of the budding yeast silent information regulator 3 (Sir3) silencing protein with the nucleosome induces a conformational change in the amino terminus of histone H4 that promotes interactions between the conserved H4 arginines 17 and 19 (R17 and R19) and nucleosomal DNA. Substitutions of H4R17 and R19 with alanine abolish silencing in vivo, but have little or no effect on binding of Sir3 to nucleosomes or histone H4 peptides in vitro. Furthermore, in both the previously reported crystal structure of the Sir3-bromo adjacent homology (BAH) domain bound to the Xenopus laevis nucleosome core particle and the crystal structure of the Sir3-BAH domain bound to the yeast nucleosome core particle described here, H4R17 and R19 make contacts with nucleosomal DNA rather than with Sir3. These results suggest that Sir3 binding generates a more stable nucleosome by clamping H4R17 and R19 to nucleosomal DNA, and raise the possibility that such induced changes in histone–DNA contacts play major roles in the regulation of chromatin structure. 相似文献
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Peptide antibody specific for the amino terminus of skeletal muscle alpha-actin. 总被引:16,自引:0,他引:16 下载免费PDF全文
J C Bulinski S Kumar K Titani S D Hauschka 《Proceedings of the National Academy of Sciences of the United States of America》1983,80(6):1506-1510
The NH2-terminal peptide of skeletal muscle alpha-actin (S alpha N peptide), which contains a primary sequence unique to this actin isozyme, was used to prepare an isozyme-specific peptide antibody. S alpha N peptide was purified from chicken breast muscle actin by preparative reverse-phase HPLC and was coupled to hemocyanin. This complex was used to immunize rabbits in order to elicit actin antibodies specific for the skeletal muscle alpha-actin isozyme. The antibody obtained, called S alpha N antibody, was reactive with S alpha N peptide and with skeletal muscle alpha-actin as well as with cardiac muscle alpha-actin. S alpha N antibody did not react with either of the actin isozymes present in smooth muscle (smooth muscle alpha and gamma) or in brain (nonmuscle beta and gamma). S alpha N antibody was used to detect muscle-specific actin in differentiating mouse and human myoblasts by using immunoblots of myoblast extracts and immunofluorescent staining of fixed cells. 相似文献
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FOXP3 interactions with histone acetyltransferase and class II histone deacetylases are required for repression 下载免费PDF全文
Li B Samanta A Song X Iacono KT Bembas K Tao R Basu S Riley JL Hancock WW Shen Y Saouaf SJ Greene MI 《Proceedings of the National Academy of Sciences of the United States of America》2007,104(11):4571-4576
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Genetic evidence for an interaction between SIR3 and histone H4 in the repression of the silent mating loci in Saccharomyces cerevisiae. 总被引:31,自引:0,他引:31 下载免费PDF全文
L M Johnson P S Kayne E S Kahn M Grunstein 《Proceedings of the National Academy of Sciences of the United States of America》1990,87(16):6286-6290
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Vicki E. Maltby Benjamin J. E. Martin Julie Brind’Amour Adam T. Chruscicki Kristina L. McBurney Julia M. Schulze Ian J. Johnson Mark Hills Thomas Hentrich Michael S. Kobor Matthew C. Lorincz LeAnn J. Howe 《Proceedings of the National Academy of Sciences of the United States of America》2012,109(45):18505-18510
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Molecular basis for keratoconus: lack of TrkA expression and its transcriptional repression by Sp3 总被引:2,自引:0,他引:2 下载免费PDF全文
Lambiase A Merlo D Mollinari C Bonini P Rinaldi AM D' Amato M Micera A Coassin M Rama P Bonini S Garaci E 《Proceedings of the National Academy of Sciences of the United States of America》2005,102(46):16795-16800
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Takahashi YH Westfield GH Oleskie AN Trievel RC Shilatifard A Skiniotis G 《Proceedings of the National Academy of Sciences of the United States of America》2011,108(51):20526-20531
Histone H3 lysine 4 (H3K4) methylation is catalyzed by the highly evolutionarily conserved multiprotein complex known as Set1/COMPASS or MLL/COMPASS-like complexes from yeast to human, respectively. Here we have reconstituted fully functional yeast Set1/COMPASS and human MLL/COMPASS-like complex in vitro and have identified the minimum subunit composition required for histone H3K4 methylation. These subunits include the methyltransferase C-terminal SET domain of Set1/MLL, Cps60/Ash2L, Cps50/RbBP5, Cps30/WDR5, and Cps25/Dpy30, which are all common components of the COMPASS family from yeast to human. Three-dimensional (3D) cryo-EM reconstructions of the core yeast complex, combined with immunolabeling and two-dimensional (2D) EM analysis of the individual subcomplexes reveal a Y-shaped architecture with Cps50 and Cps30 localizing on the top two adjacent lobes and Cps60-Cps25 forming the base at the bottom. EM analysis of the human complex reveals a striking similarity to its yeast counterpart, suggesting a common subunit organization. The SET domain of Set1 is located at the juncture of Cps50, Cps30, and the Cps60-Cps25 module, lining the walls of a central channel that may act as the platform for catalysis and regulative processing of various degrees of H3K4 methylation. This structural arrangement suggested that COMPASS family members function as exo-methylases, which we have confirmed by in vitro and in vivo studies. 相似文献
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Cis-acting elements of the sea urchin histone H2A modulator bind transcriptional factors 总被引:3,自引:1,他引:2 下载免费PDF全文
F Palla C Casano I Albanese L Anello F Gianguzza M G Di Bernardo C Bonura G Spinelli 《Proceedings of the National Academy of Sciences of the United States of America》1989,86(16):6033-6037
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Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo 总被引:17,自引:0,他引:17 下载免费PDF全文
Winkler GS Kristjuhan A Erdjument-Bromage H Tempst P Svejstrup JQ 《Proceedings of the National Academy of Sciences of the United States of America》2002,99(6):3517-3522
The elongating, hyperphosphorylated form of RNA polymerase II is associated with the Elongator complex, which has the histone acetyltransferase (HAT) Elp3 as a subunit. Here we show that, in contrast to the isolated Elp3 subunit, the activity of intact Elongator complex is directed specifically toward the amino-terminal tails of histone H3 and H4, and that Elongator can acetylate both core histones and nucleosomal substrates. The predominant acetylation sites are lysine-14 of histone H3 and lysine-8 of histone H4. The three smallest Elongator subunits--Elp4, Elp5, and Elp6--are required for HAT activity, and Elongator binds to both naked and nucleosomal DNA. By using chromatin immunoprecipitation, we show that the levels of multiply acetylated histone H3 and H4 in chromatin are decreased in vivo in yeast cells lacking ELP3. 相似文献