Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein
Autor: | P Zagouras, John K. Rose, B Crise, A Ruusala, Andrew Shaw |
---|---|
Jazyk: | angličtina |
Rok vydání: | 1989 |
Předmět: |
G protein
Macromolecular Substances Immunology Molecular Sequence Data Restriction Mapping Microbiology Vesicular stomatitis Indiana virus Viral Envelope Proteins Mutant protein Virology Protein A/G Acetylglucosaminidase Centrifugation Density Gradient Humans Amino Acid Sequence Codon Peptide sequence chemistry.chemical_classification Membrane Glycoproteins biology Base Sequence Endoplasmic reticulum biology.organism_classification Transmembrane protein Kinetics Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Biochemistry chemistry Solubility Vesicular stomatitis virus Insect Science biology.protein Electrophoresis Polyacrylamide Gel Glycolipids Glycoprotein Research Article HeLa Cells |
Popis: | The vesicular stomatitis virus glycoprotein forms noncovalently linked trimers in the endoplasmic reticulum before being transported to the Golgi apparatus. The experiments reported here were designed to determine if the extracellular domain of the glycoprotein contains structural information sufficient to direct trimer formation. To accomplish this, we generated a construct encoding G protein with the normal transmembrane and anchor sequences replaced with the sequence encoding 53 C-terminal amino acids from the Thy-1.1 glycoprotein. We show here that these sequences were able to specify glycolipid addition to the truncated G protein, probably after cleavage of 31 amino acids derived from Thy-1.1. The glycolipid-anchored G protein formed trimers and was expressed on the cell surface in a form that could be cleaved by phosphoinositol-specific phospholipase C. However, the rate of transport was reduced, compared with that of wild-type G protein. A second form of the G protein was generated by deletion of only the transmembrane and cytoplasmic domains. This mutant protein also formed trimers with relatively high efficiency and was secreted slowly from cells. |
Databáze: | OpenAIRE |
Externí odkaz: |