Alternative splicing provides a proactive mechanism for the diurnal CONSTANS dynamics in Arabidopsis photoperiodic flowering

Gil, Kyung Eun; Park, Ju Hee; Lee, Hyo Jun; Park, Young Joon; Han, Shin Jung; Kwon, Young Ju; Seo, Pil Joon; Jung, Jae Hoon; Park, Chung Mo

doi:10.1111/tpj.13351

Cited by 42 publications

(36 citation statements)

References 73 publications

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“…We reason that BTC1 or BvBBX19 alone are not able to bind to the BvFT2 promoter and that the heterodimer of mutant BvBBX19 h with the BTC1 d protein cannot bind to the BvFT2 promoter. The importance of intact domains for their binding activities was recently reported for Arabidopsis where a truncated COβ variant lacking the CCT domain lost its DNA-binding affinity 24 . The variant protein results from alternative splicing of the CO mRNA.…”

Section: Discussionmentioning

confidence: 90%

Two CONSTANS-LIKE genes jointly control flowering time in beet

Dally

Eckel

Batschauer

et al. 2018

Sci Rep

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Breeding vegetative crops (e.g. beets, cabbage, forage grasses) is challenged by two conflicting aims. For field production, flowering must be avoided while flowering and seed set is necessary for breeding and seed production. The biennial species sugar beet makes shoot elongation (‘bolting’) followed by flowering after a long period of cold temperatures. Field production in northern geographical regions starts in spring. A thickened storage root is formed only during vegetative growth. It is expected that winter beets, which are sown before winter would have a much higher yield potential. However, field production was not possible so far due to bolting after winter. We propose a strategy to breed winter beets exploiting haplotype variation at two major bolting time loci, B and B2. Both genes encode transcription factors controlling the expression of two orthologs of the Arabidopsis gene FLOWERING LOCUS T (FT). We detected an epistatic interaction between both genes because F2 plants homozygous for two B/B2 mutant alleles did not bolt even after vernalization. Fluorescence complementation studies revealed that both proteins form a heterodimer in vivo. In non-bolting plants, the bolting activator BvFT2 was completely downregulated whereas the repressor BvFT1 was upregulated which suggests that both genes acquire a CONSTANS (CO) like function in beet. Like CO, B and B2 proteins house CCT and BBX domains which, in contrast to CO are split between the two beet genes. We propose an alternative regulation of FT orthologs in beet that can be exploited to breed winter beets.

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Section: Discussionmentioning

confidence: 90%

Two CONSTANS-LIKE genes jointly control flowering time in beet

Dally

Eckel

Batschauer

et al. 2018

Sci Rep

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show abstract

“…However, alternative splicing of CO transcript generates a shorter 274-aa CO protein lacking the CCT motif at the C terminus. This truncated CO protein interacts with full-length 373-aa CO at the N-terminus, causing degradation of the 373-aa CO spliced variant to delay flowering time (Gil et al 2017). Determining how CIA2/CIL and CO interact would help establish if and how CIA2/CIL is involved in flowering regulation.…”

Section: Cia2 and Cil Interact With The Cct Motif Of Comentioning

confidence: 99%

Sequence analysis and protein interactions of Arabidopsis CIA2 and CIL proteins

Yang

Sun

2020

Bot Stud

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Background: A previous screening of Arabidopsis thaliana for mutants exhibiting dysfunctional chloroplast protein transport identified the chloroplast import apparatus (cia) gene. The cia2 mutant has a pale green phenotype and reduced rate of protein import into chloroplasts, but leaf shape and size are similar to wild-type plants of the same developmental stage. Microarray analysis showed that nuclear CIA2 protein enhances expression of the Toc75, Toc33, CPN10 and cpRPs genes, thereby up-regulating protein import and synthesis efficiency in chloroplasts. CIA2-like (CIL) shares 65% sequence identity to CIA2, suggesting that CIL and CIA2 are homologous proteins in Arabidopsis. Here, we further assess the protein interactions and sequence features of CIA2 and CIL. Results: Subcellular localizations of truncated CIA2 protein fragments in our onion transient assay demonstrate that CIA2 contains two nuclear localization signals (NLS) located at amino acids (aa) 62-65 and 291-308, whereas CIL has only one NLS at aa 47-50. We screened a yeast two-hybrid (Y2H) Arabidopsis cDNA library to search for putative CIA2interacting proteins and identified 12 nuclear proteins, including itself, CIL, and flowering-control proteins (such as CO, NF-YB1, NF-YC1, NF-YC9 and ABI3). Additional Y2H experiments demonstrate that CIA2 and CIL mainly interact with flowering-control proteins via their N-termini, but preferentially form homo-or hetero-dimers through their C-termini. Moreover, sequence alignment showed that the N-terminal sequences of CIA2, CIL and NF-YA are highly conserved. Therefore, NF-YA in the NF-Y complex could be substituted by CIA2 or CIL. Conclusions: We show that Arabidopsis CIA2 and CIL can interact with CO and NF-Y complex, so not only may they contribute to regulate chloroplast function but also to modulate flower development.

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“…However, alternative splicing of CO transcript generates a shorter 274-aa CO protein lacking the CCT motif at the C terminus. This truncated CO protein interacts with full-length 373-aa CO at the N-terminus, causing degradation of the 373-aa CO spliced variant to delay owering time (Gil et al, 2017). Determining how CIA2/CIL and CO interact would help establish if and how CIA2/CIL is involved in owering regulation.…”

Section: Con Rmation Of Protein Interactions Among Cia2-interacting Cmentioning

confidence: 99%

Sequence analysis and protein interactions of Arabidopsis CIA2 and CIL proteins

Yang

Sun

2020

Preprint

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Background: A previous screening of Arabidopsis thaliana for mutants exhibiting dysfunctional chloroplast protein transport identified the chloroplast import apparatus ( cia ) gene. The cia2 mutant has a pale green phenotype and reduced rate of protein import into chloroplasts, but leaf shape and size are similar to wild-type plants of the same developmental stage. Microarray analysis showed that nuclear CIA2 protein enhances expression of the Toc75 , Toc33 , CPN10 and cpRPs genes, thereby up-regulating protein import and synthesis efficiency in chloroplasts. CIA2-like (CIL) shares 65% sequence identity to CIA2, suggesting that CIL and CIA2 are homologous proteins in Arabidopsis. Here, we further assess the protein interactions and sequence features of CIA2 and CIL. Results: Subcellular localizations of truncated CIA2 protein fragments in our onion transient assay demonstrate that CIA2 contains two nuclear localization signals (NLS) located at amino acids (aa) 62-65 and 291-308, whereas CIL has only one NLS at aa 47-50. We screened a yeast two-hybrid (Y2H) Arabidopsis cDNA library to search for putative CIA2-interacting proteins and identified 12 nuclear proteins, including itself, CIL, and flowering-control proteins (such as CO, NF-YB1, NF-YC1, NF-YC9 and ABI3). Additional Y2H experiments demonstrate that CIA2 and CIL mainly interact with flowering-control proteins via their N-termini, but preferentially form homo- or hetero-dimers through their C-termini. Moreover, sequence alignment showed that the N-terminal sequences of CIA2, CIL and NF-YA are highly conserved. Therefore, NF-YA in the NF-Y complex could be substituted by CIA2 or CIL. Conclusions: We show that Arabidopsis CIA2 and CIL can interact with CO and NF-Y complex, so not only may they contribute to regulate chloroplast function but also to modulate flower development.

show abstract

Alternative splicing provides a proactive mechanism for the diurnal CONSTANS dynamics in Arabidopsis photoperiodic flowering

Cited by 42 publications

References 73 publications

Two CONSTANS-LIKE genes jointly control flowering time in beet

Two CONSTANS-LIKE genes jointly control flowering time in beet

Sequence analysis and protein interactions of Arabidopsis CIA2 and CIL proteins

Sequence analysis and protein interactions of Arabidopsis CIA2 and CIL proteins

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