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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1999-8-24
pubmed:abstractText
The P30 movement protein (MP) of tomato mosaic tobamovirus (ToMV) is synthesized in the early stages of infection and is phosphorylated in vivo. Here, we determined that serine 37 and serine 238 in the ToMV MP are sites of phosphorylation. MP mutants in which serine was replaced by alanine at positions 37 and 238 (LQ37A238A) or at position 37 only (LQ37A) were not phosphorylated, and mutant viruses did not infect tobacco or tomato plants. By contrast, mutation of serine 238 to alanine did not affect the infectivity of the virus (LQ238A). To investigate the subcellular localization of mutant MPs, we constructed viruses that expressed each mutant MP fused with the green fluorescent protein (GFP) of Aequorea victoria. Wild-type and mutant LQ238A MP fusion proteins showed distinct temporally regulated patterns of MP-GFP localization in protoplasts and formation of fluorescent ring-shaped infection sites on Nicotiana benthamiana. However mutant virus LQ37A MP-GFP did not show a distinct pattern of localization or formation of fluorescent rings. Pulse-chase experiments revealed that MP produced by mutant virus LQ37A was less stable than wild-type and LQ238A MPs. MP which contained threonine at position 37 was phosphorylated, but the stability of the MP in vivo was very low. These studies suggest that the presence of serine at position 37 or phosphorylation of serine 37 is essential for intracellular localization and stability of the MP, which is necessary for the protein to function.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1379865, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1392601, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1426287, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1546469, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1568243, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-16453793, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-16552920, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1726784, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1730937, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1733093, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1827229, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1943760, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1956339, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1984651, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1990065, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-1994570, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-2302736, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-2333282, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-2535549, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-2840354, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-3201760, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-3323813, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-3786131, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-5432063, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-6316652, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-6549393, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-7684009, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-7763916, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-7854443, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-8134376, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-8411345, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-8533089, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-8718621, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-9011088, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-9668131, http://linkedlifedata.com/resource/pubmed/commentcorrection/10400781-9744091
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-538X
pubmed:author
pubmed:issnType
Print
pubmed:volume
73
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6831-40
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed-meshheading:10400781-Tobacco, pubmed-meshheading:10400781-Serine, pubmed-meshheading:10400781-Alanine, pubmed-meshheading:10400781-Fluorescence, pubmed-meshheading:10400781-Aspartic Acid, pubmed-meshheading:10400781-Glutamic Acid, pubmed-meshheading:10400781-Threonine, pubmed-meshheading:10400781-Lycopersicon esculentum, pubmed-meshheading:10400781-Phosphorylation, pubmed-meshheading:10400781-Plants, Toxic, pubmed-meshheading:10400781-Intracellular Fluid, pubmed-meshheading:10400781-Viral Proteins, pubmed-meshheading:10400781-Amino Acid Sequence, pubmed-meshheading:10400781-Protoplasts, pubmed-meshheading:10400781-Binding Sites, pubmed-meshheading:10400781-Molecular Sequence Data, pubmed-meshheading:10400781-Mutagenesis, pubmed-meshheading:10400781-Luminescent Proteins, pubmed-meshheading:10400781-Recombinant Fusion Proteins
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