Conserved sequence motifs in the abiotic stress response protein late embryogenesis abundant 3

Abstract

LEA3 proteins, a family of abiotic stress proteins, are defined by the presence of a tryptophan-containing motif, which we name the W-motif. We use Pfam LEA3 sequences to search the Phytozome database to create a W-motif definition and a LEA3 sequence dataset. A comprehensive analysis of these sequences revealed four N-terminal motifs, as well as two previously undiscovered C-terminal motifs that contain conserved acidic and hydrophobic residues. The general architecture of the LEA3 sequences consisted of an N-terminal motif with a potential mitochondrial transport signal and the twin-arginine motif cut-site, followed by a W-motif and often a C-terminal motif. Analysis of species distribution of the motifs showed that one architecture was found exclusively in Commelinids, while two were distributed fairly evenly over all species. The physiochemical properties of the different architectures showed clustering in a relatively narrow range compared to the previously studied dehydrins. The evolutionary analysis revealed that the different sequences grouped into clades based on architecture, and that there appear to be at least two distinct groups of LEA3 proteins based on their architectures and physiochemical properties. The presence of LEA3 proteins in non-vascular plants but their absence in algae suggests that LEA3 may have arisen in the evolution of land plants.

The in vitro structure and functions of the disordered late embryogenesis abundant three proteins

“…The protein sequences of the four AtLEA3 proteins are shown in Figure 1(a). We have highlighted the conserved motifs we had identified in a previous bioinformatics study of this protein family, and found that this family is distributed throughout the plant kingdom, including non‐vascular plants 41 . The motif shown in red is a common feature of all LEA3 proteins and is denoted the W‐motif because of a completely conserved tryptophan residue at the N‐terminus.…”

“…The magenta shows a C-terminal motif termed the DAELR motif, which was also identified in our previous study. 41 AtLEA3-1, 3-2, and 3-3 proteins possess one copy of each motif, while AtLEA3-4 appears to lack the twin-Arg motif, the motif sometimes found after the N-terminus, and has an extra copy of the W-motif. We used several disorder servers to predict disorder propensity of the AtLEA3 proteins on a per residue basis.…”

“…We have highlighted the conserved motifs we had identified in a previous bioinformatics study of this protein family, and found that this family is distributed throughout the plant kingdom, including non-vascular plants. 41 The motif shown in red is a common feature of all LEA3 proteins and is denoted the W-motif because of a completely conserved tryptophan residue at the N-terminus. The cyan highlights the N-terminal motif, which encodes the mitochondrial transport sequence, while the green shows a motif that sometimes is found after the N-terminal motif, and likely encodes the twin-Arg cut-site motif.…”

Modular Assembly of Ordered Hydrophilic Proteins Improve Salinity Tolerance in Escherichia coli

“…Previous results suggest that the N-terminal domain of group 1 LEA proteins may be important for proper folding during dehydration [ 38 ]. Karamjeet et al predicted the conserved domains of plant G3LEA proteins and found that there are four N-terminal conserved motifs (called MAaRS, MARS, MGRX, and M [AS] [RK], respectively), which may be the signal for group 3 protein to locate mitochondria [ 39 ]. At LEA4-5, a member of group 4 of LEAs in Arabidopsis , it has been found that their N-terminal region can undergo a transition to a partially folded state and prevent enzyme inactivation, and, interestingly, the ability to gain structure under water limiting conditions is limited to the conserved region at the N-terminal, indicating the N-terminal could function as a chaperone [ 40 , 41 ].…”

Caracterización in silico y análisis de la expresión expresión génica de proteínas abundantes en la embriogénesis tardía de Agave tequilana Weber var. azul

“…La proteína LjIDP1 de Lotus japonicus es intrínsecamente desordenada en solución, pero cambia en condiciones de deshidratación o desnaturalizantes, adoptando una estructura de α-hélice y previniendo la inactivación de enzimas al evitar que formen agregados o pierdan su conformación (Haaning et al 2008). Recientemente se ha identificado que este grupo, además de contener el dominio Pfam PF03242, se definen por la presencia de un motivo W (Trp) (Singh & Graether 2020) y otros ubicados en las regiones N-y C-terminal.…”