Berks B C
Centre for Metalloprotein Spectroscopy and Biology, School of Biological Sciences, University of East Anglia, Norwich, UK.
Mol Microbiol. 1996 Nov;22(3):393-404. doi: 10.1046/j.1365-2958.1996.00114.x.
The precursor polypeptides of periplasmic proteins binding seven types of redox cofactor have unusually long signal sequences bearing a consensus (S/T)-R-R-x-F-L-K motif immediately before the hydrophobic region. Such "double-arginine' signal sequences are not, in general, found on the precursors of other periplasmic proteins. It is suggested that precursor proteins with double-arginine signal sequences share a common specialization in their export pathway. The nature of this specialization, the structure of the double-arginine signal sequences, and the possible relationship with the double-arginine signal peptide-dependent thylakoid import pathway are discussed.
结合七种氧化还原辅因子的周质蛋白的前体多肽具有异常长的信号序列，在疏水区域之前紧邻一个共有(S/T)-R-R-x-F-L-K基序。一般来说，其他周质蛋白的前体上没有这种“双精氨酸”信号序列。有人提出，具有双精氨酸信号序列的前体蛋白在其输出途径中具有共同的特殊化。本文讨论了这种特殊化的性质、双精氨酸信号序列的结构以及与双精氨酸信号肽依赖性类囊体导入途径的可能关系。
