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Fig. 1 | BMC Plant Biology

Fig. 1

From: Tomato histone H2B monoubiquitination enzymes SlHUB1 and SlHUB2 contribute to disease resistance against Botrytis cinerea through modulating the balance between SA- and JA/ET-mediated signaling pathways

Fig. 1

SlHUB1 and SlHUB2 are functional histone H2B monoubiquitination E3 ligases. a Phylogenetic tree analysis of SlHUB1 and SlHUB2 with yeast BRE (GenBank accession No. Q07457), Arabidopsis AtHUB1 (Q8RXD6) and AtHUB2 (NP_564680), and human RFN20 (NP_062538) and RFN40 (NP_001273501). Sequence alignment was performed using ClustalX 1.81 program and phylogenic tree was created and visualized using MEGA 6.06. b Amino acid alignments of the SlHUB1 and SlHUB2 RING domains with RING domains of the Arabidopsis AtHUB1 and AtHUB2 and yeast BRE. Filled triangles indicate the conserved cysteine residues, while asterisk indicates conserved histidine residue. c Recombinant SlHUB1 (right) and SlHUB2 (left) proteins have histone H2B monoubiquitination activity in vitro. Recombinant SlHUB1 and SlHUB2 and their mutants SlHUB1ΔRING and SlHUB2ΔRING were incubated with E1 enzyme, E2 enzyme (Rad6), H2B substrate and ubiquitin, separated on SDS-PAGE and detected by Western blotting using anti-ubiquitin antibody. The absences of each one of H2B, E1, E2 or ubiquitin were included as negative controls

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BMC Plant Biology

ISSN: 1471-2229

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