DISTINCTIVE PROPERTIES OF SIGNAL SEQUENCES FROM BACTERIAL LIPOPROTEINS
DISTINCTIVE PROPERTIES OF SIGNAL SEQUENCES FROM BACTERIAL LIPOPROTEINS
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DOI:
10.1093/protein/2.1.15
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发表时间:
1988-04-01
期刊:
影响因子:
--
通讯作者:
LAU, PCK
中科院分区:
文献类型:
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作者:
KLEIN, P;SOMORJAI, RL;LAU, PCK
We have compared a number of attributes (hydrophobicity, amino acid size, charge and secondary structure propensities) of signal sequences of bacterial lipoproteins with the same attributes of signal peptides from other prokaryotic proteins (non-lipoproteins). Lipoprotein leader sequences tend to be shorter, more hydrophobic and bulky, and they have stronger conformational preferences, the most conspicuous being a predicted .beta.-turn comprising position 2 or 3 of the mature protein. Another distinctive feature is a maximum in the local energy profile between positions -1 and +2. With one exception (.beta.-lactamase III), the lipoproteins do not have Pro in their signal peptides, and they tend to have fewer Ser and Thr but more Gly than non-lipoproteins. Lipoproteins also lack a net negative charge in the N-terminal regions of the mature proteins. The signal peptides of the bacteriocin plasmid-coded lysis proteins appear to be unique in that they have all the ascribed features of lipoprotein signals; these characteristics can be used to guide signal peptide mutagenesis experiments and to construct new secretion vehicles.