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|e rakwb
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|a eng
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| 100 |
1 |
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|a Cruz-Garcia, Felipe
|e verfasserin
|4 aut
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| 245 |
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|a S-RNase complexes and pollen rejection
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| 264 |
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|c 2003
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| 336 |
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|a Text
|b txt
|2 rdacontent
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| 337 |
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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| 338 |
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|a Band
|b nc
|2 rdacarrier
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| 500 |
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|a Date Completed 03.03.2003
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|a Date Revised 13.05.2019
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|a published: Print
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|a Citation Status MEDLINE
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|a Biochemical interactions between the pollen and the pistil allow plants fine control over fertilization. S-RNase-based pollen rejection is among the most widespread and best understood of these interactions. At least three plant families have S-RNase-based self-incompatibility (SI) systems, and S-RNases have also been implicated in interspecific pollen rejection. Although S-RNases determine the specificity of SI, other genes are required for the pollen rejection system to function. Progress is being made toward identifying these non-S-RNase factors. HT-protein, first identified as a non-S-RNase factor that was required for SI in Nicotiana alata, has now been implicated in other species as well. In addition, several pistil proteins bind to S-RNase in vitro. One hypothesis is that S-RNase forms a complex with these proteins in vivo that is the active form of S-RNase in pollen rejection
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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|a Research Support, U.S. Gov't, Non-P.H.S.
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| 650 |
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|a Review
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| 650 |
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7 |
|a Glycoproteins
|2 NLM
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| 650 |
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|a HT protein, Nicotiana alata
|2 NLM
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| 650 |
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|a Plant Proteins
|2 NLM
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| 650 |
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|a self-incompatibility glycoprotein, Nicotiana
|2 NLM
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| 650 |
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|a 102726-76-1
|2 NLM
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| 650 |
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| 700 |
1 |
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|a Hancock, C Nathan
|e verfasserin
|4 aut
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| 700 |
1 |
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|a McClure, Bruce
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 54(2003), 380 vom: 01. Jan., Seite 123-30
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
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|g volume:54
|g year:2003
|g number:380
|g day:01
|g month:01
|g pages:123-30
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