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231224s2012 xx |||||o 00| ||eng c |
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|a 10.1093/jxb/err323
|2 doi
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|a pubmed24n0710.xml
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|a (DE-627)NLM212891987
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|a (NLM)22068145
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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| 100 |
1 |
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|a Chen, Ming-Kun
|e verfasserin
|4 aut
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| 245 |
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|a Functional analysis reveals the possible role of the C-terminal sequences and PI motif in the function of lily (Lilium longiflorum) PISTILLATA (PI) orthologues
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|c 2012
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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| 338 |
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|a ƒa Online-Ressource
|b cr
|2 rdacarrier
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| 500 |
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|a Date Completed 10.01.2014
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|a Date Revised 21.10.2021
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a Two lily (Lilium longiflorum) PISTILLATA (PI) genes, Lily MADS Box Gene 8 and 9 (LMADS8/9), were characterized. LMADS9 lacked 29 C-terminal amino acids including the PI motif that was present in LMADS8. Both LMADS8/9 mRNAs were prevalent in the first and second whorl tepals during all stages of development and were expressed in the stamen only in young flower buds. LMADS8/9 could both form homodimers, but the ability of LMADS8 homodimers to bind to CArG1 was relatively stronger than that of LMADS9 homodimers. 35S:LMADS8 completely, and 35S:LMADS9 only partially, rescued the second whorl petal formation and partially converted the first whorl sepal into a petal-like structure in Arabidopsis pi-1 mutants. Ectopic expression of LMADS8-C (with deletion of the 29 amino acids of the C-terminal sequence) or LMADS8-PI (with only the PI motif deleted) only partially rescued petal formation in pi mutants, which was similar to what was observed in 35S:LMADS9/pi plants. In contrast, 35:LMADS9+L8C (with the addition of the 29 amino acids of the LMADS8 C-terminal sequence) or 35S:LMADS9+L8PI (with the addition of the LMADS8 PI motif) demonstrated an increased ability to rescue petal formation in pi mutants, which was similar to what was observed in 35S:LMADS8/pi plants. Furthermore, ectopic expression of LMADS8-M (with the MADS domain truncated) generated more severe dominant negative phenotypes than those seen in 35S:LMADS9-M flowers. These results revealed that the 29 amino acids including the PI motif in the C-terminal region of the lily PI orthologue are valuable for its function in regulating perianth organ formation
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|a Journal Article
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|a Research Support, Non-U.S. Gov't
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| 650 |
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|a DNA, Complementary
|2 NLM
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| 650 |
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|a MADS Domain Proteins
|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 RNA, Messenger
|2 NLM
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| 650 |
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|a RNA, Plant
|2 NLM
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| 700 |
1 |
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|a Hsieh, Wen-Ping
|e verfasserin
|4 aut
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| 700 |
1 |
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|a Yang, Chang-Hsien
|e verfasserin
|4 aut
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| 773 |
0 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g 63(2012), 2 vom: 14. Jan., Seite 941-61
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
1 |
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|g volume:63
|g year:2012
|g number:2
|g day:14
|g month:01
|g pages:941-61
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| 856 |
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|u http://dx.doi.org/10.1093/jxb/err323
|3 Volltext
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|d 63
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|e 2
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|h 941-61
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