Cer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae.
Cer1p functions as a molecular chaperone in the endoplasmic reticulum of Saccharomyces cerevisiae.
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Cer1p 在酿酒酵母内质网中充当分子伴侣。
DOI：
10.1128/mcb.19.8.5298
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发表时间：
1999
影响因子：
5.3
通讯作者：
Flynn,GC
中科院分区：
文献类型：
--
作者：
Hamilton,TG;Norris,TB;Tsuruda,PR;Flynn,GC
Cer1p/Lhs1p/Ssi1p是一种新型的hsp70相关蛋白，对于一组蛋白在酵母酵母内质网中的易位很重要。Cer1p在n端atp酶结构域与hsp70伴侣家族的氨基酸同源性非常有限，但与高度保守的hsp70肽结合结构域缺乏同源性。评估了Cer1p在蛋白质折叠和易位中的作用。在酵母中，cer1的缺失使还原前羧肽酶Y （pro-CPY）的折叠速度减慢了大约两倍。在还原条件下的野生型酵母中，可以在Cer1p的复合体中发现pro-CPY，而部分纯化的Cer1p能够直接与肽结合。总之，这表明Cer1p具有通过与未折叠的多肽直接相互作用介导的变性前cpy适当再折叠所需的陪伴活性。Cer1p肽结合和寡聚化可以被ATP的加入破坏，证实Cer1p具有功能ATP结合位点，很像Kar2p和hsp70家族的其他成员。有趣的是，将acer1依赖蛋白的信号序列替换为acer1不依赖蛋白的信号序列并没有减轻cer1的进口需求。这一结果表明，与蛋白质成熟部分的相互作用对于Cer1p的易位作用也很重要。er1rna水平在较低的温度下增加。此外，在较低的温度下，缺失对折叠和易位的影响更为严重。因此，这些结果表明Cer1p在已知需要Kar2p的过程中提供了额外的陪伴活动。然而，在较低温度下对Cer1p伴侣活性的要求似乎更高。
Cer1p/Lhs1p/Ssi1p is a novel Hsp70-related protein that is important for the translocation of a subset of proteins into the yeastSaccharomyces cerevisiaeendoplasmic reticulum. Cer1p has very limited amino acid identity to the hsp70 chaperone family in the N-terminal ATPase domain but lacks homology to the highly conserved hsp70 peptide binding domain. The role of Cer1p in protein folding and translocation was assessed. Deletion ofCER1slowed the folding of reduced pro-carboxypeptidase Y (pro-CPY) approximately twofold in yeast. In wild-type yeast under reducing conditions, pro-CPY can be found in a complex with Cer1p, while partially purified Cer1p is able to bind directly to peptides. Together, this suggests that Cer1p has a chaperoning activity required for proper refolding of denatured pro-CPY which is mediated by direct interaction with the unfolded polypeptide. Cer1p peptide binding and oligomerization could be disrupted by addition of ATP, confirming that Cer1p possesses a functional ATP binding site, much like Kar2p and other members of the hsp70 family. Interestingly, replacing the signal sequence of aCER1-dependent protein with that of aCER1-independent protein did not relieve the requirement ofCER1for import. This result suggests that an interaction with the mature portion of the protein also is important for the translocation role of Cer1p. TheCER1RNA levels increase at lower temperatures. In addition, the effects of deletion on folding and translocation are more severe at lower temperatures. Therefore, these results suggest that Cer1p provides an additional chaperoning activity in processes known to require Kar2p. However, there appears to be a greater requirement for Cer1p chaperone activity at lower temperatures.
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BIP/KAR2P在酵母中羧肽酶y折叠期间用作分子伴侣。
影响因子：
7.8
作者：
SIMONS, JF;FERRONOVICK, S;ROSE, MD;HELENIUS, A
通讯作者：
HELENIUS, A
影响因子：
56.9
作者：
FLYNN, GC;CHAPPELL, TG;ROTHMAN, JE
通讯作者：
ROTHMAN, JE
含有 Sec61p 复合物同源物的第二个三聚复合物在跨酿酒酵母 ER 膜的蛋白质转运中发挥作用。
影响因子：
11.4
作者：
K. Finke;K. Plath;S. Panzner;S. Prehn;T. Rapoport;E. Hartmann;T. Sommer
通讯作者：
T. Sommer
DOI：
10.1083/jcb.120.1.95
发表时间：
1993-01
期刊：
The Journal of cell biology
影响因子：
--
作者：
Brodsky JL;Hamamoto S;Feldheim D;Schekman R
通讯作者：
Schekman R
酵母信息素受体内吞作用所需的顺式和反式作用功能
影响因子：
7.8
作者：
N. Davis;J. Horecka;G. Sprague
通讯作者：
G. Sprague