Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum

Daniel J. Chin; Gregorio Gil; David W. Russell; Laura Liscum; Kenneth L. Luskey; Sandip K. Basu; Hiroto Okayama; Paul Berg; Joseph L. Goldstein; Michael S. Brown

doi:10.1038/308613a0

Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum

Daniel J. Chin, Gregorio Gil, David W. Russell, Laura Liscum, Kenneth L. Luskey, Sandip K. Basu, Hiroto Okayama, Paul Berg, Joseph L. Goldstein, Michael S. Brown

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

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Abstract

The nucleotide sequence of a 4.8-kilobase mRNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase, the endoplasmic reticulum enzyme that controls cholesterol biosynthesis, shows that it is a protein of 887 amino acids (molecular weight 97,092) which contains three potential sites for asparagine-linked glycosylation. The reductase is a transmembrane glycoprotein, but in contrast to many other transmembrane glycoproteins, it lacks a cleavable or Hydrophobie NH₂-terminal signal sequence.

Original language	English (US)
Pages (from-to)	613-617
Number of pages	5
Journal	Nature
Volume	308
Issue number	5960
DOIs	https://doi.org/10.1038/308613a0
State	Published - Dec 1 1984

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title = "Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum",

abstract = "The nucleotide sequence of a 4.8-kilobase mRNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase, the endoplasmic reticulum enzyme that controls cholesterol biosynthesis, shows that it is a protein of 887 amino acids (molecular weight 97,092) which contains three potential sites for asparagine-linked glycosylation. The reductase is a transmembrane glycoprotein, but in contrast to many other transmembrane glycoproteins, it lacks a cleavable or Hydrophobie NH2-terminal signal sequence.",

author = "Chin, {Daniel J.} and Gregorio Gil and Russell, {David W.} and Laura Liscum and Luskey, {Kenneth L.} and Basu, {Sandip K.} and Hiroto Okayama and Paul Berg and Goldstein, {Joseph L.} and Brown, {Michael S.}",

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T1 - Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum

AU - Chin, Daniel J.

AU - Gil, Gregorio

AU - Russell, David W.

AU - Liscum, Laura

AU - Luskey, Kenneth L.

AU - Basu, Sandip K.

AU - Okayama, Hiroto

AU - Berg, Paul

AU - Goldstein, Joseph L.

AU - Brown, Michael S.

PY - 1984/12/1

Y1 - 1984/12/1

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AB - The nucleotide sequence of a 4.8-kilobase mRNA for hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase, the endoplasmic reticulum enzyme that controls cholesterol biosynthesis, shows that it is a protein of 887 amino acids (molecular weight 97,092) which contains three potential sites for asparagine-linked glycosylation. The reductase is a transmembrane glycoprotein, but in contrast to many other transmembrane glycoproteins, it lacks a cleavable or Hydrophobie NH2-terminal signal sequence.

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Nucleotide sequence of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase, a glycoprotein of endoplasmic reticulum

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