Mutation of host DnaJ homolog inhibits brome mosaic virus negative-strand RNA synthesis. Export

@article{citeulike:1258191, abstract = {The replication of positive-strand RNA viruses involves not only viral proteins but also multiple cellular proteins and intracellular membranes. In both plant cells and the yeast Saccharomyces cerevisiae, brome mosaic virus (BMV), a member of the alphavirus-like superfamily, replicates its RNA in endoplasmic reticulum (ER)-associated complexes containing viral 1a and 2a proteins. Prior to negative-strand RNA synthesis, 1a localizes to ER membranes and recruits both positive-strand BMV RNA templates and the polymerase-like 2a protein to ER membranes. Here, we show that BMV RNA replication in S. cerevisiae is markedly inhibited by a mutation in the host YDJ1 gene, which encodes a chaperone Ydj1p related to Escherichia coli DnaJ. In the ydj1 mutant, negative-strand RNA accumulation was inhibited even though 1a protein associated with membranes and the positive-strand RNA3 replication template and 2a protein were recruited to membranes as in wild-type cells. In addition, we found that in ydj1 mutant cells but not wild-type cells, a fraction of 2a protein accumulated in a membrane-free but insoluble, rapidly sedimenting form. These and other results show that Ydj1p is involved in forming BMV replication complexes active in negative-strand RNA synthesis and suggest that a chaperone system involving Ydj1p participates in 2a protein folding or assembly into the active replication complex.}, address = {Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan.}, author = {Tomita, Y. and Mizuno, T. and D\'{\i}ez, J. and Naito, S. and Ahlquist, P. and Ishikawa, M.}, citeulike-article-id = {1258191}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/12584324}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=12584324}, issn = {0022-538X}, journal = {J Virol}, keywords = {bromo, dnaj, replication}, month = {March}, number = {5}, pages = {2990--2997}, posted-at = {2007-04-27 01:32:51}, priority = {2}, title = {Mutation of host DnaJ homolog inhibits brome mosaic virus negative-strand RNA synthesis.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/12584324}, volume = {77}, year = {2003} }

TY - JOUR ID - citeulike:1258191 L3 - citeulike-article-id:1258191 N2 - The replication of positive-strand RNA viruses involves not only viral proteins but also multiple cellular proteins and intracellular membranes. In both plant cells and the yeast Saccharomyces cerevisiae, brome mosaic virus (BMV), a member of the alphavirus-like superfamily, replicates its RNA in endoplasmic reticulum (ER)-associated complexes containing viral 1a and 2a proteins. Prior to negative-strand RNA synthesis, 1a localizes to ER membranes and recruits both positive-strand BMV RNA templates and the polymerase-like 2a protein to ER membranes. Here, we show that BMV RNA replication in S. cerevisiae is markedly inhibited by a mutation in the host YDJ1 gene, which encodes a chaperone Ydj1p related to Escherichia coli DnaJ. In the ydj1 mutant, negative-strand RNA accumulation was inhibited even though 1a protein associated with membranes and the positive-strand RNA3 replication template and 2a protein were recruited to membranes as in wild-type cells. In addition, we found that in ydj1 mutant cells but not wild-type cells, a fraction of 2a protein accumulated in a membrane-free but insoluble, rapidly sedimenting form. These and other results show that Ydj1p is involved in forming BMV replication complexes active in negative-strand RNA synthesis and suggest that a chaperone system involving Ydj1p participates in 2a protein folding or assembly into the active replication complex. IS - 5 JF - J Virol SN - 0022-538X AD - Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan. EP - 2997 TI - Mutation of host DnaJ homolog inhibits brome mosaic virus negative-strand RNA synthesis. VL - 77 SP - 2990 KW - bromo KW - dnaj KW - replication AU - Tomita, Y AU - Mizuno, T AU - Díez, J AU - Naito, S AU - Ahlquist, P AU - Ishikawa, M PY - 2003/03// UR - http://view.ncbi.nlm.nih.gov/pubmed/12584324 ER -