Species‐specific variation in signal peptide design Implications for protein secretion in foreign hosts
- 27 February 1989
- journal article
- research article
- Published by Wiley in FEBS Letters
- Vol. 244 (2) , 439-446
- https://doi.org/10.1016/0014-5793(89)80579-4
Abstract
Secretory signal peptides from individual prokaryotic and eukaryotic species have been analyzed, and the lengths and amino acid compositions of the positively charged amino‐terminal region, the central hydrophobic region, and the carboxy‐terminal cleavage‐region have been compared. We find distinct differences between species in all three regions. Implications for protein secretion in foreign hosts are discussed.Keywords
This publication has 90 references indexed in Scilit:
- Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranesNature, 1988
- Defective Escherichia coli signal peptides function in yeastMolecular Microbiology, 1988
- Nucleotide sequence of the maltohexaose-producing amylase gene from an alkalophilic sp. #707 and structural similarity to liquefying type α-amylasesBiochemical and Biophysical Research Communications, 1988
- Translocation in yeast and mammalian cells: not all signal sequences are functionally equivalent.The Journal of cell biology, 1987
- Electron microscopic and biophysical studies of liposome membrane structures to characterize similar features of the membranes of Streptomyces hygroscopicusBiochimica et Biophysica Acta (BBA) - Biomembranes, 1987
- Signal sequencesJournal of Molecular Biology, 1985
- The complete nucleotide sequence of the xylanase gene (xynA) of Bacillus pumilusFEBS Letters, 1984
- A genetic system for analysis of staphylococcal nucleaseGene, 1983
- Structure of a yeast pheromone gene (MFα): A putative α-factor precursor contains four tandem copies of mature α-factorCell, 1982
- Conformational preferences of amino acids in globular proteinsBiochemistry, 1978