PREDICTING THE TOPOLOGY OF EUKARYOTIC MEMBRANE-PROTEINS
PREDICTING THE TOPOLOGY OF EUKARYOTIC MEMBRANE-PROTEINS
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DOI：
10.1111/j.1432-1033.1993.tb17885.x
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发表时间：
1993-05-01
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影响因子：
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通讯作者：
VONHEIJNE, G
中科院分区：
文献类型：
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作者：
SIPOS, L;VONHEIJNE, G
我们发现所谓的“正向内部”规则，即在跨膜蛋白中，带正电荷的氨基酸往往比胞外氨基酸更普遍的观察结果[von Heijne，G.(1986)EMBO J.5,3021-3027]，似乎适用于多跨真核膜蛋白中的所有极性片段，无论它们在序列中的位置如何，因此可以结合疏水性分析来预测它们的跨膜拓扑结构。此外，正如其他人所建议的那样，我们确认第一跨膜段的净电荷差与其取向有很好的相关性[Hartmann，E.，Rapoport，T.A.和Loish，H.F.(1989)Proc。纳特·阿卡德。SCI。美国86,5786-5790]，长极节段的氨基酸组成也可以用来预测它们的胞质或胞外位置[Nakashima，H.和Nishikawa，K.(1992)FEBS Lett]。303、141-146]。我们提出了一种基于这些方法相结合的方法来解决真核膜蛋白的拓扑预测问题。
We show that the so-called 'positive inside' rule, i.e. the observation that positively charged amino acids tend to be more prevalent in cytoplasmic than in extra-cytoplasmic segments in transmembrane proteins [von Heijne, G. (1986) EMBO J. 5, 3021-3027], seems to hold for all polar segments in multi-spanning eukaryotic membrane proteins irrespective of their position in the sequence and hence can be used in conjunction with hydrophobicity analysis to predict their transmembrane topology. Further, as suggested by others, we confirm that the net charge difference across the first transmembrane segment correlates well with its orientation [Hartmann, E., Rapoport, T. A. and Lodish, H. F. (1989) Proc. Natl Acad. Sci. USA 86, 5786-5790], and that the overall amino-acid composition of long polar segments can also be used to predict their cytoplasmic or extra-cytoplasmic location [Nakashima, H. and Nishikawa, K. (1992) FEBS Lett. 303, 141-146]. We present an approach to the topology prediction problem for eukaryotic membrane proteins based on a combination of these methods.