Early synthesis of membrane protein after bacteriophage T4 infection
| Autor: | Andrew D. Beckey, Charles F. Earhart, Judith L. Wulff |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Vesicle-associated membrane protein 8
Time Factors Ultraviolet Rays Immunology Biology Tritium Microbiology Coliphages Surface-Active Agents Viral Proteins Bacterial Proteins Leucine Virology Host outer membrane Escherichia coli Carbon Radioisotopes Integral membrane protein Peripheral membrane protein Cell Membrane DNA Viruses Transmembrane protein Molecular Weight Radiation Effects Membrane protein Biochemistry Solubility Insect Science Bacterial Viruses Virulence-related outer membrane protein family Electrophoresis Polyacrylamide Gel Bacterial outer membrane Peptides |
| Zdroj: | Journal of virology. 14(4) |
| ISSN: | 0022-538X |
| Popis: | Proteins that associate with cellular membrane during the first 5 min after infection with bacteriophage T4 were examined. Several procedures, including electrophoretic separations in three sodium dodecyl sulfate polyacrylamide gel systems and inhibition of host protein synthesis by UV irradiation, were employed to distinguish host-specified proteins from those induced by T4. Residual host protein synthesis was found to account for much of the new protein in preparations of the total membrane and for almost all of the newly synthesized protein in the outer membrane. Preliminary evidence indicates that the synthesis of some host membrane proteins is shut off less rapidly than is host synthesis of soluble protein. One host-directed polypeptide of the outer membrane was unique in that its synthesis or incorporation into the membrane was preferentially inhibited by infection. Also, it was found that the detergent Sarkosyl solubilizes all early T4 membrane proteins; this observation provides the basis for a simple procedure for distinguishing phage proteins from host outer membrane proteins. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|