About: Cloning, expression and characterization of serine palmitoyltransferase (SPT)-like gene subunit (LCB2) from marine Emiliania huxleyi virus (Coccolithovirus)

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About: Cloning, expression and characterization of serine palmitoyltransferase (SPT)-like gene subunit (LCB2) from marine Emiliania huxleyi virus (Coccolithovirus) Goto Sponge NotDistinct Permalink

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Cloning, expression and characterization of serine palmitoyltransferase (SPT)-like gene subunit (LCB2) from marine Emiliania huxleyi virus (Coccolithovirus)
Creator	Liu, Jingwen Cai, Yiqin Liu, Xuhong Tianling, Zheng
source	PMC
abstract	The authors have isolated and characterized a novel serine palmitoyltransferase (SPT)-like gene in marine Emiliania huxleyi virus (EhV-99B1). The open-reading frame (ORF) of EhV99B1-SPT encoded a protein of 496 amino acids with a calculated molecular mass of 96 kDa and Ip 6.01. The results of sequence analysis showed that there was about 31%–45% identity in amino acid sequence with other organisms. The maximum likelihood phylogenetic tree suggested that the EhV99B1-SPT gene possibly horizontally transferred from the eukaryote. Hydrophobic profiles of deduced amino acid sequences suggested a hydrophobic, globular and membrane-associated protein with five transmembrane domains (TMDs) motifs. Several potential N-linked glycosylation sites were presented in SPT. These results suggested that EhV99B1-SPT was an integral endoplasmic reticulum membrane protein. Despite lower sequence identity, the secondary and three-dimensional structures predicted showed that the “pocket” structure element composed of 2α-helices and 4β-sheets was the catalytic center of this enzyme, with a typical conserved “TFTKSFG” active site in the N-terminal region and was very close to those of prokaryotic organisms. However, the N-terminal domain of EhV99B1-SPT most closely resembled the LCB2 catalysis subunit and the C-terminal domain most closely resembled the LCB1 regulatory subunit of other organisms which together formed a spherical molecule. This “chimera” was highly similar to the prokaryotic homologous SPT. For a functional identification, the EhV99B1-LCB2 subunit gene was expressed in Escherichia coli, which resulted in significant accumulation of new sphingolipid in E. coli cells.
has issue date	2012-12-13(xsd:dateTime)
bibo:doi	10.1007/s13131-012-0259-z
bibo:pmid	32226188
has license	no-cc
sha1sum (hex)	782e8c610b8c353a34c6686622c387972f2452e7
schema:url	https://doi.org/10.1007/s13131-012-0259-z
resource representing a document's title	Cloning, expression and characterization of serine palmitoyltransferase (SPT)-like gene subunit (LCB2) from marine Emiliania huxleyi virus (Coccolithovirus)
has PubMed Central identifier	PMC7097000
has PubMed identifier	32226188
schema:publication	Hai Yang Xue Bao
resource representing a document's body	covid:782e8c610b8c353a34c6686622c387972f2452e7#body_text
is schema:about of	named entity 'molecule' named entity 'membrane protein' named entity 'molecular mass' named entity 'Emiliania huxleyi' named entity 'sequence identity' named entity 'composed' named entity 'protein' named entity 'Hydrophobic' named entity 'spherical' named entity 'prokaryotic' named entity 'gene' named entity 'Emiliania huxleyi' named entity 'SPT' named entity 'chimera' named entity 'eukaryote' named entity 'active site' named entity 'prokaryotic' named entity 'endoplasmic reticulum' named entity 'three-dimensional structures' named entity 'Coccolithovirus' named entity 'eukaryote' named entity 'Ip 6' named entity 'N-terminal domain' named entity 'TMDs' named entity 'serine palmitoyltransferase' named entity 'phylogenetic tree' named entity 'Escherichia coli' named entity 'Emiliania huxleyi' named entity 'gene' named entity 'gene' named entity 'serine palmitoyltransferase' named entity 'genome sequenced' named entity 'sphingolipid' named entity 'restriction endonucleases' named entity 'sterol' named entity 'genetic material' named entity 'ceramide' named entity 'fungi' named entity 'amino acids' named entity 'gene' named entity 'open reading frame' named entity 'lipids' named entity 'yeast' named entity 'Virus' named entity 'apoptosis' named entity 'ceramide' named entity 'N-linked glycosylation sites' named entity 'phylogeny' named entity 'agarose gel' named entity 'Coccolithoviridae' named entity 'prokaryotic' named entity 'kDa' named entity 'mol/L' named entity 'Red Queen' named entity 'host cell' named entity 'PLP' named entity 'evolution' named entity 'inoculated' named entity 'protein' named entity 'horizontally transferred' named entity 'assay' named entity 'Biotechnology' named entity 'National Centre' named entity 'amino acid sequence' named entity 'eukaryotic' named entity 'lysis' named entity 'E. huxleyi' named entity 'Norway' named entity 'Plymouth' named entity 'TaKaRa' named entity 'pyridinium' named entity 'ORF' named entity 'random coil' named entity 'viruses' named entity 'lipids' named entity 'Algal' named entity 'programmed cell death' named entity 'catalytic center'

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