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. 2009 Mar;149(3):1529–1540. doi: 10.1104/pp.108.135053

Table I.

Putative in vivo sumoylation substrates of Arabidopsis

Criteria for inclusion of a protein were robust detection in preparations, absence from control preparations, and apparent molecular mass, as detailed in the text. n.t., Not tested.

Identifier Characteristics ΨKxD/Ea In Vivo Conjugate to: In Vitro Sumoylationb
RNA-dependent processes
    At1g29400 AML5; has one RRM2 domain, two RRM1 domains 1 (1) SUM3 Yes
    At3g56860 Contains two RRM1 domains 1 (0) SUM1 Yes
    At2g43970 Contains an LA domain 0 (1) SUM1 No
    At2g47020 Translation release factor 1 (2) SUM3 n.t.
    At3g60240 eIF4G 4 (2) SUM3 n.t.
Chromatin-related processes
    At1g55300 TAF7 (TFIID subunit) 0 (0) SUM3, -5 Yes
    At2g19480 Nucleosome assembly factor 2 (0) SUM1 Yes
    At5g08450 Contains an Rxt3 domain 3 (10) SUM3 Yes
    At5g39660 zfDOF transcription factor 1 (1) SUM1 n.t.
    At5g43130 TFIID subunit 2 (4) SUM1 n.t.
Others
    At1g27430 Contains a GYF domain 1 (4) SUM1, -3 n.t.
    At1g64330 Contains a KIP domain, coiled-coil region 2 (1) SUM1, -3 n.t.
    At5g13480 FY; WD40 repeat protein 0 (0) SUM1, -3 n.t.
    At5g52300 RD29B desiccation induced 3 (2) SUM1 n.t.
a

In addition to canonical SUMO attachment sites (Ψ is an aliphatic hydrophobic residue, x indicates any residue, D/E is either Asp or Glu), many proteins contain nearly canonical sequences as further potential SUMO attachment sites (number of such sites is given in parentheses; www.abgent.com/doc/sumoplot).

b

The in vitro sumoylation reactions referred to here used SUMO1 and its variant SUMO1 Q90A with identical results.