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Florigen and Its Homologs of FT/CETS/PEBP/RKIP/YbhB Family May Be the Enzymes of Small Molecule Metabolism: Review of the Evidence

Overview
Journal BMC Plant Biol
Publisher Biomed Central
Specialty Biology
Date 2022 Jan 28
PMID 35086479
Authors
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Abstract

Background: Flowering signals are sensed in plant leaves and transmitted to the shoot apical meristems, where the formation of flowers is initiated. Searches for a diffusible hormone-like signaling entity ("florigen") went on for many decades, until a product of plant gene FT was identified as the key component of florigen in the 1990s, based on the analysis of mutants, genetic complementation evidence, and protein and RNA localization studies. Sequence homologs of FT protein are found throughout prokaryotes and eukaryotes; some eukaryotic family members appear to bind phospholipids or interact with the components of the signal transduction cascades. Most FT homologs are known to share a constellation of five charged residues, three of which, i.e., two histidines and an aspartic acid, are located at the rim of a well-defined cavity on the protein surface.

Results: We studied molecular features of the FT homologs in prokaryotes and analyzed their genome context, to find tentative evidence connecting the bacterial FT homologs with small molecule metabolism, often involving substrates that contain sugar or ribonucleoside moieties. We argue that the unifying feature of this protein family, i.e., a set of charged residues conserved at the sequence and structural levels, is more likely to be an enzymatic active center than a catalytically inert ligand-binding site.

Conclusions: We propose that most of FT-related proteins are enzymes operating on small diffusible molecules. Those metabolites may constitute an overlooked essential ingredient of the florigen signal.

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References
1.
Luo H, Lin Y, Gao F, Zhang C, Zhang R . DEG 10, an update of the database of essential genes that includes both protein-coding genes and noncoding genomic elements. Nucleic Acids Res. 2013; 42(Database issue):D574-80. PMC: 3965060. DOI: 10.1093/nar/gkt1131. View

2.
El-Gebali S, Mistry J, Bateman A, Eddy S, Luciani A, Potter S . The Pfam protein families database in 2019. Nucleic Acids Res. 2018; 47(D1):D427-D432. PMC: 6324024. DOI: 10.1093/nar/gky995. View

3.
Mima J, Hayashida M, Fujii T, Narita Y, Hayashi R, Ueda M . Structure of the carboxypeptidase Y inhibitor IC in complex with the cognate proteinase reveals a novel mode of the proteinase-protein inhibitor interaction. J Mol Biol. 2005; 346(5):1323-34. DOI: 10.1016/j.jmb.2004.12.051. View

4.
Guo C, Chang T, Sun T, Wu Z, Dai Y, Yao H . Anti-leprosy drug Clofazimine binds to human Raf1 kinase inhibitory protein and enhances ERK phosphorylation. Acta Biochim Biophys Sin (Shanghai). 2018; 50(10):1062-1067. DOI: 10.1093/abbs/gmy095. View

5.
Sohn E, Rojas-Pierce M, Pan S, Carter C, Serrano-Mislata A, Madueno F . The shoot meristem identity gene TFL1 is involved in flower development and trafficking to the protein storage vacuole. Proc Natl Acad Sci U S A. 2007; 104(47):18801-6. PMC: 2141857. DOI: 10.1073/pnas.0708236104. View