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Review
, 18 (7)

An Update on Jacalin-Like Lectins and Their Role in Plant Defense

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Review

An Update on Jacalin-Like Lectins and Their Role in Plant Defense

Lara Esch et al. Int J Mol Sci.

Abstract

Plant lectins are proteins that reversibly bind carbohydrates and are assumed to play an important role in plant development and resistance. Through the binding of carbohydrate ligands, lectins are involved in the perception of environmental signals and their translation into phenotypical responses. These processes require down-stream signaling cascades, often mediated by interacting proteins. Fusing the respective genes of two interacting proteins can be a way to increase the efficiency of this process. Most recently, proteins containing jacalin-related lectin (JRL) domains became a subject of plant resistance responses research. A meta-data analysis of fusion proteins containing JRL domains across different kingdoms revealed diverse partner domains ranging from kinases to toxins. Among them, proteins containing a JRL domain and a dirigent domain occur exclusively within monocotyledonous plants and show an unexpected high range of family member expansion compared to other JRL-fusion proteins. Rice, wheat, and barley plants overexpressing OsJAC1, a member of this family, are resistant against important fungal pathogens. We discuss the possibility that JRL domains also function as a decoy in fusion proteins and help to alert plants of the presence of attacking pathogens.

Keywords: JRL domain; chimeric protein; decoy; dirigent protein; fusion protein; plant resistance.

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Proportional distribution of JRL domain containing proteins by superfamilies, among different kingdoms and taxa. JRL proteins (PF01419) of different taxonomic groups (bacteria, oomycetes, fungi, eudicotyledons, Liliopsida (monocotyledons) and other plants) were identified using UniProt. Domains were identified using NCBI Batch Web CD-Search Tool. Results were filtered for superfamilies as depicted. Below each pie chart the total number of JRL proteins that were found in the corresponding taxonomic group is given. Number next to the respective pie segment represent percentage of JRL domain containing proteins in depicted superfamily. Since chimeric JRL proteins may contain more than one partner domain, the respective protein might occur in different superfamilies, increasing the total percentage to >100. CRA: CT11-RanBPM; CTLH: C-terminal to LisH motif, alpha-helical motif of unknown function; DUF2235: domain of unknown function 2235; EEP: Exonuclease-Endonuclease-Phosphatase; ETX/MTX2: Clostridium epsilon toxin ETX/Bacillus mosquitocidal toxin MTX2; FBA_1: F-box associated 1; FU: Furin-like repeats; HHH_5: Helix-hairpin-helix domain; LisH: type-1-like homology motif; LRR_4: Leucin-rich repeats (2 copies); MACPF: Membrane-attack complex/Perforin domain; NPP1: necrosis-inducing protein; NUDE_C: NUDE protein, C-terminal conserved region; PI-PLCc_GDPD_SF: Catalytic domain of phosphoinositide-specific phospholipase C-like phosphodiesterases; PKc: Protein Kinases, catalytic domain; P-loop_NTPase: P-loop containing Nucleoside triphosphate hydrolases; PolY: Y-family of DNA-Polymerases; PPR: PPR repeat, unknown function; RICIN: Ricin-type beta trefoil; RX-CC: coiled-coil domain of the potato virus X resistance protein and similar proteins; ZnMc: Zinc-dependent metalloproteases.

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