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- Title
Functional Analysis of the GPI Transamidase Complex by Screening for Amino Acid Mutations in Each Subunit.
- Authors
Liu, Si-Si; Jin, Fei; Liu, Yi-Shi; Murakami, Yoshiko; Sugita, Yukihiko; Kato, Takayuki; Gao, Xiao-Dong; Kinoshita, Taroh; Hattori, Motoyuki; Fujita, Morihisa
- Abstract
Glycosylphosphatidylinositol (GPI) anchor modification is a posttranslational modification of proteins that has been conserved in eukaryotes. The biosynthesis and transfer of GPI to proteins are carried out in the endoplasmic reticulum. Attachment of GPI to proteins is mediated by the GPI-transamidase (GPI-TA) complex, which recognizes and cleaves the C-terminal GPI attachment signal of precursor proteins. Then, GPI is transferred to the newly exposed C-terminus of the proteins. GPI-TA consists of five subunits: PIGK, GPAA1, PIGT, PIGS, and PIGU, and the absence of any subunit leads to the loss of activity. Here, we analyzed functionally important residues of the five subunits of GPI-TA by comparing conserved sequences among homologous proteins. In addition, we optimized the purification method for analyzing the structure of GPI-TA. Using purified GPI-TA, preliminary single particle images were obtained. Our results provide guidance for the structural and functional analysis of GPI-TA.
- Subjects
FUNCTIONAL analysis; POST-translational modification; PROTEIN precursors; AMINO acids; ENDOPLASMIC reticulum; ENDONUCLEASES
- Publication
Molecules, 2021, Vol 26, Issue 18, p5462
- ISSN
1420-3049
- Publication type
Article
- DOI
10.3390/molecules26185462