Membrane translocation and insertion of NH2‐terminally anchored γ‐glutamyl transpeptidase require a signal recognition particle

FEBS Letters

Tate, Suresh S.¹  Nash, Barbara¹ 

[1] Department of Biochemistry, Cornell University Medical College, New York, NY 10021, USA

关键词: γ-Glutamyl transpeptidase;    Brush border enzyme;    Membrane insertion;    Signal sequence;    Signal recognition particle;   

DOI  :  10.1016/0014-5793(87)81423-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The two subunits of the renal brush border enzyme, γ-glutamyl transpeptidase (EC 2.3.2.2), are derived from a single-chain propeptide. The membrane-spanning domain consists of a hydrophobic sequence near its NH₂-terminus and the protein is oriented with its NH₂-terminus on the cytoplasmic side. The enzyme is synthesized without a cleavable signal sequence. Translocation and insertion of this enzyme have been shown to be dependent on the signal recognition particle and presumably require the same translocation machinery that other secretory and membrane proteins use for these processes.

【 授权许可】

Unknown