GIFT domains: linking eukaryotic intraflagellar transport and glycosylation to bacterial gliding.

Scott Beatson; CP Ponting

doi:10.1016/j.tibs.2004.06.002

GIFT domains: linking eukaryotic intraflagellar transport and glycosylation to bacterial gliding.

Scott Beatson, CP Ponting

Research output: Contribution to journal › Article

18 Citations (Scopus)

Abstract

We describe GIFT [for GldG, intraflagellar transport (IFT)] domains in the flavobacterial gliding protein GldG and eukaryotic IFT-52. In eukaryotes, domain homologues are also found in the eukaryotic oligosaccharyltransferase complex and in subtilisin kexin isozyme-1 (SKI-1 or S1P). A distant evolutionary relationship to periplasmic-binding proteins hints that GIFT domains might possess oligosaccharide-binding functions.

Original language	English
Pages (from-to)	396-9
Number of pages	4
Journal	Trends in Biochemical Sciences
Volume	29
Issue number	8
DOIs	https://doi.org/10.1016/j.tibs.2004.06.002
Publication status	Published - 1 Aug 2004

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10.1016/j.tibs.2004.06.002

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title = "GIFT domains: linking eukaryotic intraflagellar transport and glycosylation to bacterial gliding.",

abstract = "We describe GIFT [for GldG, intraflagellar transport (IFT)] domains in the flavobacterial gliding protein GldG and eukaryotic IFT-52. In eukaryotes, domain homologues are also found in the eukaryotic oligosaccharyltransferase complex and in subtilisin kexin isozyme-1 (SKI-1 or S1P). A distant evolutionary relationship to periplasmic-binding proteins hints that GIFT domains might possess oligosaccharide-binding functions.",

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AU - Beatson, Scott

AU - Ponting, CP

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N2 - We describe GIFT [for GldG, intraflagellar transport (IFT)] domains in the flavobacterial gliding protein GldG and eukaryotic IFT-52. In eukaryotes, domain homologues are also found in the eukaryotic oligosaccharyltransferase complex and in subtilisin kexin isozyme-1 (SKI-1 or S1P). A distant evolutionary relationship to periplasmic-binding proteins hints that GIFT domains might possess oligosaccharide-binding functions.

AB - We describe GIFT [for GldG, intraflagellar transport (IFT)] domains in the flavobacterial gliding protein GldG and eukaryotic IFT-52. In eukaryotes, domain homologues are also found in the eukaryotic oligosaccharyltransferase complex and in subtilisin kexin isozyme-1 (SKI-1 or S1P). A distant evolutionary relationship to periplasmic-binding proteins hints that GIFT domains might possess oligosaccharide-binding functions.

U2 - 10.1016/j.tibs.2004.06.002

DO - 10.1016/j.tibs.2004.06.002

M3 - Article

C2 - 15288869

VL - 29

SP - 396

EP - 399

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 8

ER -

GIFT domains: linking eukaryotic intraflagellar transport and glycosylation to bacterial gliding.

Abstract

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