The E3-10.4K protein of adenovirus is an integral membrane protein that is partially cleaved between Ala22 and Ala23 and has a Ccyt orientation.
The E3-10.4K protein of adenovirus is an integral membrane protein that is partially cleaved between Ala22 and Ala23 and has a Ccyt orientation.
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腺病毒的E3-10.4K蛋白是一种整合膜蛋白，在Ala22和Ala23之间部分切割，具有Ccyt方向。
DOI：
10.1016/0042-6822(92)90302-6
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发表时间：
1992
期刊：
影响因子：
3.7
通讯作者：
Wold,WS
中科院分区：
文献类型：
--
作者：
Krajcsi,P;Tollefson,AE;Anderson,CW;Stewart,AR;Carlin,CR;Wold,WS
在腺病毒感染的细胞中，需要Ad 2 E3-10.4K蛋白与E3-14.5K蛋白一起下调表皮生长因子受体。在某些条件下，这两种蛋白质也是防止肿瘤坏死因子细胞溶解所必需的。10.4K是一种91个氨基酸的膜结合蛋白，在SDS-PAGE上以上下两条带迁移。我们在这里表明，上面的带是主要的翻译产物，在AUG 2173开始在E3转录单位的Ad 2。通过微粒体相关蛋白酶在残基Ala 22和Ala 23之间的蛋白水解切割，上部条带被缓慢加工（>4小时完成）成下部条带。上带和下带在丰度上变得相等，之后它们非常稳定。体内衍生的上带的N-末端未被阻断以进行测序，并且其保留其起始Met。10.4K在其N末端附近具有疏水结构域（H1），其可能是膜插入的信号序列;该信号的切割是非典型的，因为其在体内不是共翻译的，并且其不完全。10.4K具有位于残基35-60内的第二疏水结构域（H2）。H2似乎是一个跨膜（终止转移）结构域，因为在pH11.5提取后，10.4K的上带和下带都与膜结合，因为这两条带都被Triton X-114提取到去污剂相中，而且当用蛋白酶K消化含10.4K的微粒体时，这两条带的大小仅部分减少。这些蛋白酶K消化的条带用抗残基19-34的抗肽抗血清免疫沉淀，但不与抗残基68-80或77-91的抗血清免疫沉淀，表明两个10.4K条带都在膜中取向，C-末端在细胞质中。我们的结论是，10.4K的下带是I型双位膜蛋白，并建议，上带是一个多位膜蛋白与H1和H2的疏水结构域跨越膜。
The Ad2 E3-10.4K protein is required together with the E3-14.5K protein to down-regulate the epidermal growth factor receptor in adenovirus-infected cells. Both proteins are also required to prevent tumor necrosis factor cytolysis under certain conditions. 10.4K is a 91 amino acid membrane-associated protein that migrates as two bands, upper and lower, on SDS-PAGE. We show here that the upper band is the primary translation product which initiates at AUG2173in the E3 transcription unit of Ad2. The upper band is processed slowly (>4 hr to complete) into the lower band by proteolytic cleavage between residues Ala22and Ala23by a microsome-associated protease. The upper and lower bands become equal in abundance, after which they are very stable. The N-terminus of the in vivo-derived upper band is not blocked to sequencing and it retains its initiating Met. 10.4K has a hydrophobic domain (H1) near its N-terminus that is probably a signal sequence for membrane insertion; cleavage of this signal is atypical because it was not contranslational in vivo and it was not complete. 10.4K has a second hydrophobic domain (H2) located within residues 35–60. H2 appears to be a transmembrane (stop transfer) domain because both the upper and the lower 10.4K bands remained associated with membranes after extraction at pH 11.5, because both bands were extracted into the detergent phase with Triton X-114, and because both bands were only partially reduced in size when 10.4K-containing microsomes were digested with proteinase K. These proteinase K-digested bands were immunoprecipitated with an antipeptide antiserum against residues 19–34 but not with an antiserum against residues 68–80 or 77–91, indicating that both 10.4K bands are orientated in the membrane with the C-terminus in the cytoplasm. We conclude that the lower band of 10.4K is a type I bitopic membrane protein and suggest that the upper band is a polytopic membrane protein with both the H1 and the H2 hydrophobic domains spanning the membrane.
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[36] 人腺病毒：生长、纯化和转染测定
影响因子：
--
作者：
M. Green;W. Wold
通讯作者：
W. Wold
腺病毒 2 感染细胞的同种异体识别减少。
影响因子：
4.4
作者：
M. Andersson;A. McMichael;P. A. Peterson
通讯作者：
P. A. Peterson
影响因子：
5.6
作者：
PERLMAN, D;HALVORSON, HO
通讯作者：
HALVORSON, HO
6700 MW 膜蛋白由 2 型腺病毒 E3 区编码。
影响因子：
3.7
作者：
Wilson-Rawls,J;Saha,SK;Krajcsi,P;Tollefson,AE;Gooding,LR;Wold,WS
通讯作者：
Wold,WS
影响因子：
5.4
作者：
HARTER, ML;SHANMUGAM, G;GREEN, M
通讯作者：
GREEN, M