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Expression and Activity of Chimeric Molecules between Human UDP-Galactose Transporter and CMP-Sialic Acid Transporter

Aoki, Kazuhisa ; Sun-Wada, Ge-Hong ; Segawa, Hiroaki ; Yoshioka, Shigemi ; Ishida, Nobuhiro ; Kawakita, Masao

Journal of biochemistry (Tokyo), 1999-11, Vol.126 (5), p.940-950 [Peer Reviewed Journal]

England: Oxford University Press

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Title:
Expression and Activity of Chimeric Molecules between Human UDP-Galactose Transporter and CMP-Sialic Acid Transporter
Author: Aoki, Kazuhisa ; Sun-Wada, Ge-Hong ; Segawa, Hiroaki ; Yoshioka, Shigemi ; Ishida, Nobuhiro ; Kawakita, Masao
Subjects: Animals ; Base Sequence ; Biological Transport, Active ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; chimeric transporter ; CHO Cells ; CMP-sialic acid transporter ; Cricetinae ; Cytidine Monophosphate N-Acetylneuraminic Acid - metabolism ; DNA Primers - genetics ; DNA, Recombinant - genetics ; Endoplasmic Reticulum - metabolism ; Gene Expression ; Golgi apparatus ; Golgi Apparatus - metabolism ; Humans ; In Vitro Techniques ; Membrane Proteins - chemistry ; Membrane Proteins - genetics ; Membrane Proteins - metabolism ; Monosaccharide Transport Proteins - chemistry ; Monosaccharide Transport Proteins - genetics ; Monosaccharide Transport Proteins - metabolism ; Mutation ; nucleo-tide-sugar transporter ; Nucleotide Transport Proteins ; Protein Structure, Secondary ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - metabolism ; RNA, Messenger - genetics ; RNA, Messenger - metabolism ; UDP-galactose transporter ; Uridine Diphosphate Galactose - metabolism
Is Part Of: Journal of biochemistry (Tokyo), 1999-11, Vol.126 (5), p.940-950
Notes: ArticleID:126.5.940
istex:5C04092B47FBA63EC8FEE44ECCCF49F887ABC587
3To whom correspondence should be sent
ark:/67375/HXZ-PDTNFK7N-6
1This work was supported in part by Grants-in-Aid for Scientific Research 11159220, 11480172, and 11877024 from the Ministry of Education, Science, Sports and Culture of Japan and by research grants from Kirin Brewery Co. Ltd., Japan and Mizutani Foundation for Glycoscience.
ObjectType-Article-1
SourceType-Scholarly Journals-1
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Description: Human UDP-galactose transporter (hUGTl) and CMP-sialic acid transporter (hCST) are related Golgi proteins with eight putative transmembrane helices predicted by computer analysis. We constructed chimeric molecules in which segments of various lengths from the C- or N-terminus of hUGTl were replaced by corresponding portions of hCST. The chimeras were transiently expressed in UGT-deficient mutant Lec8 cells, and their UGT activity was assessed by the binding of GS-II lectin to the transfected cells. The replacement of either the N- or C-terminal cytoplasmic segment by that of hCST did not affect the expression or activity of hUGTl. A chimera in which the eighth helix and the C-terminal tail were replaced also retained the UGT activity, indicating that this helix is not involved in the determination of substrate specificity. In contrast, three types of chimeras, in which the first helix, the first and the second helices, and a segment from the seventh helix to the C-terminus were replaced, respectively, were expressed very infrequently in the transfected cells, and had no UGT activity. They are likely folded incorrectly and degraded by a quality-control system, since the amounts of their mRNAs were normal and the proteins were mainly localized in the ER. The first and the seventh helices are important for the stability of the transporter protein.
Publisher: England: Oxford University Press
Language: English

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Expression and Activity of Chimeric Molecules between Human UDP-Galactose Transporter and CMP-Sialic Acid Transporter

Aoki, Kazuhisa ; Sun-Wada, Ge-Hong ; Segawa, Hiroaki ; Yoshioka, Shigemi ; Ishida, Nobuhiro ; Kawakita, Masao

England: Oxford University Press

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