rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1998-3-25
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pubmed:abstractText |
Self-incompatibility RNases (S-RNases) are an allelic series of style glycoproteins associated with rejection of self-pollen in solanaceous plants. The nucleotide sequences of S-RNase alleles from several genera have been determined, but the structure of the gene products has only been described for those from Nicotiana alata. We report on the N-glycan structures and the disulfide bonding of the S3-RNase from wild tomato (Lycopersicon peruvianum) and use this and other information to construct a model of this molecule. The S3-RNase has a single N-glycosylation site (Asn-28) to which one of three N-glycans is attached. S3-RNase has seven Cys residues; six are involved in disulfide linkages (Cys-16-Cys-21, Cys-46-Cys-91, and Cys-166-Cys-177), and one has a free thiol group (Cys-150). The disulfide-bonding pattern is consistent with that observed in RNase Rh, a related RNase for which radiographic-crystallographic information is available. A molecular model of the S3-RNase shows that four of the most variable regions of the S-RNases are clustered on one surface of the molecule. This is discussed in the context of recent experiments that set out to determine the regions of the S-RNase important for recognition during the self-incompatibility response.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-1498421,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-1633875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-2237440,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-2364940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-2535547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-2594090,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-3064654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-5492953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-7098932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-7390980,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-7866034,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-8066136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-8122904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-8563138,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-8749320,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-8922956,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-8954155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-9161037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9489006-9414554
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0032-0889
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
116
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
463-9
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pubmed:dateRevised |
2010-9-10
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pubmed:meshHeading |
pubmed-meshheading:9489006-Amino Acid Sequence,
pubmed-meshheading:9489006-Carbohydrate Sequence,
pubmed-meshheading:9489006-Disulfides,
pubmed-meshheading:9489006-Lycopersicon esculentum,
pubmed-meshheading:9489006-Mass Spectrometry,
pubmed-meshheading:9489006-Models, Molecular,
pubmed-meshheading:9489006-Molecular Sequence Data,
pubmed-meshheading:9489006-Polysaccharides,
pubmed-meshheading:9489006-Protein Conformation,
pubmed-meshheading:9489006-Ribonucleases
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pubmed:year |
1998
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pubmed:articleTitle |
Structural analysis and molecular model of a self-incompatibility RNase from wild tomato.
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pubmed:affiliation |
Plant Cell Biology Research Centre, School of Botany, University of Melbourne, Parkville, VIC, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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