Structural Basis for Multi-specificity of MRG Domains.
Structural Basis for Multi-specificity of MRG Domains.
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DOI：
10.1016/j.str.2015.03.020
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发表时间：
2015-06-02
期刊：
影响因子：
5.7
通讯作者：
Radhakrishnan, Ishwar
中科院分区：
文献类型：
--
作者：
Xie, Tao;Zmyslowski, Adam M.;Zhang, Yongbo;Radhakrishnan, Ishwar
Chromatin-binding proteins play vital roles in the assembly and recruitment of multi-subunit complexes harboring effector proteins to specific genomic loci. MRG15, a chromodomain-containing chromatin-binding protein, recruits diverse chromatin-associated complexes that regulate gene transcription, DNA repair, and RNA splicing. Previous studies with Pf1, another chromatin-binding subunit of the Sin3S/Rpd3S histone deacetylase complex, defined the sequence and structural requirements for interactions with the MRG15 MRG domain, a common target of diverse subunits in the aforementioned complexes. We now show that MRGBP, a member of the Tip60/NuA4 histone acetyltransferase complex, engages the same two surfaces of the MRG domain as Pf1. High-affinity interactions occur via a bipartite structural motif including an FxLP sequence motif. MRGBP shares little sequence and structural similarity with Pf1, yet, targets similar pockets on the surface of the MRG domain, mimicking Pf1 in its interactions. Our studies shed light into how MRG domains have evolved to bind diverse targets.
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影响因子：
5.6
作者：
Kumar, Ganesan Senthil;Chang, William;Xie, Tao;Patel, Anand;Zhang, Yongbo;Wang, Gang Greg;David, Gregory;Radhakrishnan, Ishwar
通讯作者：
Radhakrishnan, Ishwar
影响因子：
10.5
作者：
Lalonde ME;Cheng X;Côté J
通讯作者：
Côté J
影响因子：
16
作者：
Joshi, AA;Struhl, K
通讯作者：
Struhl, K
DOI：
10.1080/21541264.2014.995571
发表时间：
2014
期刊：
Transcription
影响因子：
--
作者：
Cheng X;Côté J
通讯作者：
Côté J
DOI：
10.1107/s0907444998003254
发表时间：
1998-09-01
期刊：
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
影响因子：
--
作者：
Brunger, AT;Adams, PD;Warren, GL
通讯作者：
Warren, GL