Interactions of an Arabidopsis RanBPM homologue with LisH-CTLH domain proteins revealed high conservation of CTLH complexes in eukaryotes

Table 1 Proteins copurified with AtRanBPM are members of CTLH complexes

Protein name	AGI number	Band No.	MW [kDa]	No. peptides	Sequence coverage [%]	Aranet/ATTED-II	Members of CTLH complex in other organisms
AtRanBPM	At1g35470	1	52	17/41	41/60		RanBPM [Q96S59] Gid1/Vid30 [P53076]***
LisH and RanBPM domain-containing protein	At1g61150	6	25	8/26	41/82	-/+	Twa1 [Q9NWU2]Gid8 [P40208]*
LisH/CRA/RING-U-box domain-containing protein	At3g55070	4	48	10/17	28/31	+/-	MAEA [Q7L5Y9]Gid9p [P40492]**
LisH/CRA/RING-U-box domain-containing protein	At4g37880	5	44	9/8	32/22	+/-	RMD5 [Q9H871]Gid2 [Q12508]**
Transducin/WD40 domain-containing protein	At5g08560	2	66	17/14	38/31	+/-	WDR26 [Q9H7D7]
Transducin/WD40 domain-containing protein	At5g43920	3	60	6/4	13/7	+/-	WDR26 [Q9H7D7]

Proteins (for band numbering see Figure 4A) copurified with AtRanBPM protein were identified by both MALDI-MS and LC-MALDI-MS/MS analysis. The values before and after the slash in the columns “No. peptides” and “Sequence coverage” refer to MALDI-MS and LC-MALDI-MS/MS data, respectively. Homologues of human CTLH-complex members reported by Kobayashi et al., [15] (*), proteins in the complex described by Umeda et al. [12] (**), yeast homologues in the Gid complex published by Regelmann et al. [16] (***).

ISSN: 1471-2229