Localization and biochemical characterization of alfalfa mosaic virus replication complexes.
Replication complexes were isolated from alfalfa mosaic virus-infected tobacco protoplasts. Most of the RNA-synthesizing activity appears to colocalize with the intact chloroplasts upon sucrose-gradient centrifugation of cellular homogenates. Further analysis of these replication complexes showed that the enzyme is strongly associated with the outside of the chloroplasts, the endogenous template being well protected against ribonuclease action. RNA polymerase activity is sensitive to protease treatment of intact chloroplast fraction showing that an essential part of the enzyme complex is facing the in vitro medium, and probably the cytosol in vivo.
Institute of Molecular Plant Sciences, Gorlaeus Laboratories, Leiden University, The Netherlands.
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De Graaff
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Coscoy
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Jaspars
D002451:Cell Compartmentation; D002736:Chloroplasts / Q000378:metabolism; D003600:Cytosol / Q000378:metabolism; D007425:Intracellular Membranes / Q000378:metabolism; D000455:Medicago sativa / Q000382:microbiology*; D009029:Mosaic Viruses / Q000254:growth & development*; D010947:Plants, Toxic; D011523:Protoplasts / Q000382:microbiology; D012367:RNA, Viral / Q000096:biosynthesis*; D012324:RNA-Dependent RNA Polymerase / Q000378:metabolism; D014026:Nicotiana / Q000382:microbiology; D014779:Virus Replication
D012367:RNA, Viral; D012324:RNA-Dependent RNA Polymerase