A folding zone in the ribosomal exit tunnel for Kv1.3 helix formation.

A folding zone in the ribosomal exit tunnel for Kv1.3 helix formation.
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DOI:
10.1016/j.jmb.2009.12.059
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发表时间:
2010-03-12
影响因子:
5.6
通讯作者:
Deutsch C
Deutsch C
中科院分区:
生物学2区
文献类型:
--
作者:
Tu LW;Deutsch C

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虽然现在已经清楚蛋白质二级结构可以在早期获得,而新生肽位于核糖体出口通道内,但控制天然多位蛋白折叠的原理尚未阐明。我们现在报告了一个广泛的调查本地Kv1.3,电压门控K+通道,包括跨膜和连接器的序列合成的片段。这些天然片段仅在位于隧道最后20度的容许前庭中矢量地(N-至C-末端)形成螺旋。天然接头序列类似地在该前庭中折叠。最后,在核糖体中获得的二级结构保留在易位子中。这些发现来自对多种天然跨膜和接头序列的可及性研究,因此可能适用于一般蛋白质生物发生。
Although it is now clear that protein secondary structure can be acquired early, while the nascent peptide resides within the ribosomal exit tunnel, the principles governing folding of native polytopic proteins have not yet been elucidated. We now report an extensive investigation of native Kv1.3, a voltage-gated K+ channel, including transmembrane and linker segments synthesized in sequence. These native segments form helices vectorially (N- to C-terminus) only in a permissive vestibule located in the last 20Å of the tunnel. Native linker sequences similarly fold in this vestibule. Finally, secondary structure acquired in the ribosome is retained in the translocon. These findings emerge from accessibility studies of a diversity of native transmembrane and linker sequences and may therefore be applicable to protein biogenesis in general.
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