TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei

Yeonchul Hong; Kisaburo Nagamune; Kazuhito Ohishi; Yasu S. Morita; Hisashi Ashida; Yusuke Maeda; Taroh Kinoshita

doi:10.1016/j.febslet.2005.12.075

TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei

Yeonchul Hong
, Kisaburo Nagamune
, Kazuhito Ohishi
, Yasu S. Morita
, Hisashi Ashida
, Yusuke Maeda
, Taroh Kinoshita

Department of Medicine

The University of Osaka

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

Abstract

Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.

Original language	English
Pages (from-to)	603-606
Number of pages	4
Journal	FEBS Letters
Volume	580
Issue number	2
DOIs	https://doi.org/10.1016/j.febslet.2005.12.075
State	Published - 23 Jan 2006

Keywords

Endoplasmic reticulum
Glycosylphosphatidylinositol
Intermolecular disulfide bond
Post-translational modification
Transamidase

Access to Document

10.1016/j.febslet.2005.12.075

Cite this

@article{0ee3172a88a8409fb8e1787172bd34e7,

title = "TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei",

abstract = "Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.",

keywords = "Endoplasmic reticulum, Glycosylphosphatidylinositol, Intermolecular disulfide bond, Post-translational modification, Transamidase",

author = "Yeonchul Hong and Kisaburo Nagamune and Kazuhito Ohishi and Morita, \{Yasu S.\} and Hisashi Ashida and Yusuke Maeda and Taroh Kinoshita",

year = "2006",

month = jan,

day = "23",

doi = "10.1016/j.febslet.2005.12.075",

language = "English",

volume = "580",

pages = "603--606",

journal = "FEBS Letters",

issn = "0014-5793",

publisher = "John Wiley and Sons Inc.",

number = "2",

}

TY - JOUR

T1 - TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei

AU - Hong, Yeonchul

AU - Nagamune, Kisaburo

AU - Ohishi, Kazuhito

AU - Morita, Yasu S.

AU - Ashida, Hisashi

AU - Maeda, Yusuke

AU - Kinoshita, Taroh

PY - 2006/1/23

Y1 - 2006/1/23

N2 - Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.

AB - Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.

KW - Endoplasmic reticulum

KW - Glycosylphosphatidylinositol

KW - Intermolecular disulfide bond

KW - Post-translational modification

KW - Transamidase

UR - https://www.scopus.com/pages/publications/30644476355

U2 - 10.1016/j.febslet.2005.12.075

DO - 10.1016/j.febslet.2005.12.075

M3 - Article

C2 - 16405969

AN - SCOPUS:30644476355

SN - 0014-5793

VL - 580

SP - 603

EP - 606

JO - FEBS Letters

JF - FEBS Letters

IS - 2

ER -

TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this