Transmembrane segments form tertiary hairpins in the folding vestibule of the ribosome.
Transmembrane segments form tertiary hairpins in the folding vestibule of the ribosome.
复制标题
跨膜片段在核糖体的折叠前庭中形成三级发夹。
DOI:
10.1016/j.jmb.2013.09.013
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发表时间:
2014-01-09
影响因子:
5.6
通讯作者:
Deutsch, Carol
中科院分区:
文献类型:
--
作者:
Tu, LiWei;Khanna, Pooja;Deutsch, Carol
关键词:
Folding of membrane proteins begins in the ribosome as the peptide is elongated. During this process, the nascent peptide navigates along 100 Å of tunnel from the peptidyltransferase center to the exit port. Proximal to the exit port is a ‘folding vestibule’ that permits the nascent peptide to compact and explore conformational space for potential tertiary folding partners. The latter occurs for cytosolic subdomains, but has not yet been shown for transmembrane segments. We now demonstrate, using an accessibility assay and an improved, intramolecular crosslinking assay, that the helical transmembrane S3b-S4 hairpin (‘paddle’) of a voltage-gated potassium (Kv) channel, a critical region of the Kv voltage sensor, forms in the vestibule. S3-S4 hairpin interactions are detected at an early stage of Kv biogenesis. Moreover, this vestibule hairpin is consistent with a closed-state conformation of the Kv channel in the plasma membrane.
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