U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression.
U1 snRNA directly interacts with polypyrimidine tract-binding protein during splicing repression.
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DOI：
10.1016/j.molcel.2011.02.012
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发表时间：
2011-03-04
期刊：
影响因子：
16
通讯作者：
Black DL
中科院分区：
文献类型：
--
作者：
Sharma S;Maris C;Allain FH;Black DL
c-src N1外显子的剪接受到多嘧啶束结合蛋白（PTB或PTBP1）的抑制。在外显子抑制期间，U1 snRNP正确地结合到N1外显子5 '剪接位点，但由于PTB的存在而失去活性。通过检查5 '剪接位点的核酸酶保护模式，我们发现U1的相互作用被相邻的PTB改变。有趣的是，uv交联鉴定了pre- mrna结合的PTB和U1 snRNA之间的直接接触。EMSA、ITC和NMR研究表明，PTB RRMs 1和2结合了U1 snRNA茎环4富含嘧啶的内部环。PTB/U1相互作用阻止了U1 snRNP与下游剪接体成分的进一步组装。剪接调节因子和剪接体的snRNA组分之间的这种精确的相互作用指向了一系列不同的剪接调节机制。
Splicing of the c-src N1 exon is repressed by the polypyrimidine tract binding protein (PTB or PTBP1). During exon repression, the U1 snRNP binds properly to the N1 exon 5′ splice site but is made inactive by the presence of PTB. Examining the patterns of nuclease protection at this 5′ splice site, we find that the interaction of U1 is altered by the adjacent PTB. Interestingly, UV-crosslinking identifies a direct contact between the pre-mRNA-bound PTB and the U1 snRNA. EMSA, ITC and NMR studies show that PTB RRMs 1 and 2 bind the pyrimidine-rich internal loop of U1 snRNA stem loop 4. The PTB/U1 interaction prevents further assembly of the U1 snRNP with spliceosomal components downstream. This precise interaction between a splicing regulator and an snRNA component of the spliceosome points to a range of different mechanisms for splicing regulation.
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