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|a 10.1093/jxb/erae337
|2 doi
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|a pubmed24n1495.xml
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|a (DE-627)NLM376010487
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|a (NLM)39113673
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|a (PII)erae337
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Pinoti, Vitor F
|e verfasserin
|4 aut
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|a SCI1, a flower regulator of cell proliferation, and its partners NtCDKG2 and NtRH35 interact with the splicing machinery
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|c 2024
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
|b c
|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Revised 08.08.2024
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|a published: Print-Electronic
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|a Citation Status Publisher
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|a © The Author(s) 2024. Published by Oxford University Press on behalf of the Society for Experimental Biology. All rights reserved. For commercial re-use, please contact reprintsoup.com for reprints and translation rights for reprints. All other permissions can be obtained through our RightsLink service via the Permissions link on the article page on our site—for further information please contact journals.permissions@oup.com.
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|a Successful plant reproduction depends on the adequate development of flower organs controlled by cell proliferation and other processes. The SCI1 gene regulates cell proliferation and affects the final size of the female reproductive organ. To unravel the molecular mechanism exerted by SCI1 in cell proliferation control, we searched for its interaction partners through semi-in vivo pulldown experiments, uncovering a cyclin-dependent kinase, NtCDKG;2. Bimolecular fluorescence complementation (BiFC) and co-localization experiments showed that SCI1 interacts with NtCDKG;2 and its cognate NtCyclin L in nucleoli and splicing speckles. The screening of a yeast two-hybrid (Y2H) cDNA library using SCI1 as bait revealed a novel DEAD-box RNA helicase (NtRH35). The interaction between the NtCDKG;2-NtCyclin L complex, and NtRH35 was also shown. Subcellular localization experiments showed that SCI1, NtRH35, and the NtCDKG;2-NtCyclin L complex associate with each other within splicing speckles. The Y2H screening of NtCDKG;2 and NtRH35 identified the conserved spliceosome components U2a', NKAP, and CACTIN. This work presents SCI1 and its interactors NtCDKG;2-NtCyclin L complex, and NtRH35 as new spliceosome-associated proteins. Our findings reveal a network of interactions and suggest that SCI1 may regulate cell proliferation through the splicing process. This study provides new valuable insights into the intricate molecular pathways governing plant development
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|a Journal Article
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|a 2
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|a CACTIN
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|a CDKG
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|a Cyclin L
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|a DEAD-box RNA helicase RH35
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|a NKAP
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|a Pol II-CTD
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|a RBP11
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|a RBP7
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|a U2a'
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|a spliceosome
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|a Ferreira, Pedro B
|e verfasserin
|4 aut
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|a Strini, Edward J
|e verfasserin
|4 aut
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|a Lubini, Greice
|e verfasserin
|4 aut
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|a Thomé, Vanessa
|e verfasserin
|4 aut
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|a Cruz, Joelma O
|e verfasserin
|4 aut
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|a Aziani, Rodrigo
|e verfasserin
|4 aut
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|a Quiapim, Andréa C
|e verfasserin
|4 aut
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|a Pinto, Andressa P A
|e verfasserin
|4 aut
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|a Araujo, Ana Paula U
|e verfasserin
|4 aut
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| 700 |
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|a De Paoli, Henrique C
|e verfasserin
|4 aut
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|a Pranchevicius, Maria Cristina S
|e verfasserin
|4 aut
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| 700 |
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|a Goldman, Maria Helena S
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Journal of experimental botany
|d 1985
|g (2024) vom: 08. Aug.
|w (DE-627)NLM098182706
|x 1460-2431
|7 nnns
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| 773 |
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|g year:2024
|g day:08
|g month:08
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|u http://dx.doi.org/10.1093/jxb/erae337
|3 Volltext
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