Related Experiment Video
Updated: Jul 11, 2026

RNAi Trigger Delivery into Anopheles gambiae Pupae
Published on: March 8, 2016
Yarrowia lipolytica SRP receptor alpha-subunit
1Institute of Marine Resources, University of California, One Shields Avenue, Davis, CA 95616, USA.
Abstract:
The Yarrowia lipolytica SRP101 homologue encoding the signal recognition particle (SRP) receptor alpha-subunit (SRalphap) was cloned using degenerate primers designed for conserved GTP-binding domains. Sequencing of 2814 nucleotides revealed an open reading frame of 1671 base pairs encoding a putative protein of 557 amino acids with a predicted molecular mass of 61 kDa. Like other SRP101 homologues, Y. lipolytica SRP101 contains a highly conserved C-terminal GTP binding site. It has 44%, 34% and 22% sequence identity with S. cerevisiae, mammalian and Escherichia coli homologues, respectively. As found for SRP protein subunits of Y. lipolytica, SRP101 is important but not essential for cell growth. A conditional mutation in SRP101 affected synthesis/translocation of alkaline extracellular protease and Kar2p consistent with Srp101p functioning as an SRP receptor subunit. The SRP101 sequence has been deposited in GenBank under Accession No. AF132597.
Related Concept Videos
Directing Proteins to the Rough Endoplasmic Reticulum
Cell Signaling in Plants

