bioRxiv Science⌕ Search

Biology subjects

Trofimov, K.

Publications and source records attributed to Trofimov, K..

2 recordsLinked to original sources

The small iron-deficiency-induced protein OLIVIA and its relation to the bHLH transcription factor POPEYE

Iron (Fe) is a crucial micronutrient needed in many metabolic processes. To balance needs and potential toxicity, plants control the amount of Fe they take up and allocate to leaves and seeds during their development. One important regulator of this process is POPEYE (PYE). PYE is a Fe deficiency-induced key bHLH transcription factor (TF) for allocation of internal Fe in plants. In the absence of PYE, there is altered Fe translocation and plants develop a leaf chlorosis. NICOTIANAMINE SYNTHASE4 (NAS4), FERRIC-REDUCTION OXIDASE3 (FRO3), and ZINC-INDUCED FACILITATOR1 (ZIF1) genes are expressed at higher level in pye-1 indicating that PYE represses these genes. PYE activity is controlled in a yet unknown manner. Here, we show that a small Fe deficiency-induced protein OLIVIA (OLV) can interact with PYE. OLV has a conserved C-terminal motif, that we named TGIYY. Through deletion mapping, we pinpointed that OLV TGIYY and several regions of PYE can be involved in the protein interaction. An OLV overexpressing (OX) mutant line exhibited an enhanced NAS4 gene expression. This was a mild Fe deficiency response phenotype that was related to PYE function. Leaf rosettes of olv mutants remained smaller than those of wild type, indicating that OLV promotes plant growth. Taken together, our study identified a small protein OLV as a candidate that may connect aspects of Fe homeostasis with regulation of leaf growth. HighlightsO_LIOLIVIA (OLV), a small protein, can interact with the bHLH transcription factor POPEYE (PYE) C_LIO_LIOLV has a conserved motif, named TGIYY, that can be involved in protein interaction with PYE C_LIO_LIOLV mutant plants have mild phenotypes related with PYE and NAS4 regulation. C_LIO_LIOLV promotes rosette growth. C_LI

plant biology↗

FER-LIKE IRON DEFICIENCY-INDUCED TRANSCRIPTION FACTOR (FIT) accumulates in homo- and heterodimeric complexes in dynamic and inducible nuclear condensates associated with speckle components

Some nuclear proteins undergo condensation, but the functional importance remains often unclear. The basic helix-loop-helix (bHLH) FER-LIKE IRON DEFICIENCY-INDUCED TRANSCRIPTION FACTOR (FIT) integrates internal and external signals to control iron acquisition and growth. The previously described C-terminal residues Ser271/272 allow FIT to form active complexes with subgroup Ib bHLH factors such as bHLH039. FIT has lower nuclear mobility than mutant FITmSS271AA. Here, we show that FIT undergoes a light-inducible subnuclear partitioning into nuclear condensates that we termed FIT nuclear bodies (NBs). FIT NB characteristics were examined using a standardized FIT NB analysis procedure coupled with different types of quantitative and qualitative microscopy-based approaches. FIT condensates were reversible and likely formed by liquid-liquid phase separation. FIT accumulated preferentially in FIT NBs versus nucleoplasm when engaged in protein complexes with itself and with bHLH039. FITmSS271AA, instead, localized to NBs with different dynamics. FIT colocalized with splicing and light signaling NB markers. The NB-inducing light conditions were linked with active FIT and elevated FIT target gene expression in roots. Hence, we conclude that inducible, highly dynamic FIT condensates form preferentially when transcription factor complexes are active. Inducible FIT nuclear condensates may affect nuclear mobility and integrate environmental and Fe nutrition signals. HighlightsO_LIFIT undergoes light-induced, reversible condensation and localizes to nuclear bodies (NBs), likely via liquid-liquid phase separation C_LIO_LIFunctionally relevant Ser271/272 defines an intrinsically disordered region and influences NB formation dynamics C_LIO_LINBs are preferential sites for FIT dimerization with FIT and bHLH039, dependent on Ser271/272 C_LIO_LIFIT NBs colocalize with NB markers related to splicing and light signaling C_LIO_LILight conditions inducing NBs are linked with active FIT, in agreement with elevated FIT target gene expression in roots C_LI

plant biology↗