Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera.

Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera. Research Abstract Details 

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Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera. Abstract Text:

Gongshe Han,Kenneth Gable,Lianying Yan,Michael J Allen,William H Wilson,Prasun Moitra,Jeffrey M Harmon,Teresa M Dunn,

The genus Coccolithovirus is a recently discovered group of viruses that infect the globally important marine calcifying microalga Emiliania huxleyi. Surprisingly, the viral genome contains a cluster of putative sphingolipid biosynthetic genes not found in other viral genus. To address the role of these genes in viral pathogenesis, the ehv050 gene predicted to encode a serine palmitoyltransferase (SPT), the first and rate-limiting enzyme of sphingolipid biosynthesis, was expressed and characterized in Saccharomyces cerevisiae. We show that the encoded protein is indeed a fully functional, endoplasmic reticulum-localized, single-chain SPT. In eukaryotes SPT is a heterodimer comprised of long chain base 1 (LCB1) and LCB2 subunits. Sequence alignment and mutational analysis showed that the N-terminal domain of the viral protein most closely resembled the LCB2 subunit and the C-terminal domain most closely resembled the LCB1 subunit. Regardless of whether the viral protein was expressed as a single polypeptide or as two independent domains, it exhibited an unusual preference for myristoyl-CoA rather than palmitoyl-CoA. This preference was reflected by the increased presence of C16-sphingoid bases in yeast cells expressing the viral protein. The occurrence of a single-chain SPT suggested to us that it might be possible to create other fusion SPTs with unique properties. Remarkably, when the two subunits of the yeast SPT were thus expressed, the single-chain chimera was functional and displayed a novel substrate preference. This suggests that expression of other multisubunit membrane proteins as single-chain chimera could provide a powerful approach to the characterization of integral membrane proteins.

Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera. Publishing Authors By Initials

G Han,K Gable,L Yan,MJ Allen,WH Wilson,P Moitra,JM Harmon,TM Dunn,

For similar proteins: viral proteins research abstracts see: proteins: viral proteins research

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Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 39935-42

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 6

MONTH: 11

YEAR: 2006

Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera. Keywords Mesh Terms:

KEYWORDS: Viral Proteins

MESH TERMS: genetics

Chemical & Substance for Abstract: Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera. Information

Substance Name: Serine C-Palmitoyltransferase

Registry Number: EC 2.3.1.50

Grant and Affiliation Information for Expression of a novel marine viral single-chain serine palmitoyltransferase and construction of yeast and mammalian single-chain chimera.

AFFILIATION: Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20184, USA.

Country: United States

AGENCY: United States NINDS

GRANT: NS47717

ACRONYM: NS

MEDLINETA: J Biol Chem

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