A signal peptide with a proline next to the cleavage site inhibits leader peptidase when present in a sec‐independent protein

FEBS Letters

Nilsson, IngMarie¹  von Heijne, Gunnar¹ 

[1] Department of Molecular Biology, Karolinska Institute Center for Structural Biochemistry, NOVUM, S-141 57 Huddinge, Sweden

关键词: Leader peptidase;    Protein secretion;    Signal peptide;    sec pathway;   

DOI  :  10.1016/0014-5793(92)80124-Y

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Proline residues are rarely found in the three most C-terminal positions of bacterial signal peptides, and have never been found in position +1 immediately following the cleavage site. It was recently shown that a Pro⁺¹ mutation in the E. coli maltose binding protein precursor not only prevents cleavage of the signal peptide but also inhibits the leader peptidase enzyme, resulting in cessation of cell growth (Barkocy-Gallagher, G.A. and Bassford, P.J. (1992) J. Biol. Chem. (in press)). Since maltose binding protein is dependent on the sec machinery for translocation across the inner membrane, it was not clear if this ‘Pro⁺¹’ effect was restricted to sec-dependent proteins, or whether it applies also to proteins that do not require the sec functions for translocation. We now present data suggesting that the striking phenotypic effects of Pro⁺¹ mutations can be elicited also by sec-independent proteins.

【 授权许可】

Unknown