Table I.

VDAC1 interactors found by yeast two-hybrid screening

NameAccession number
DnaJ (Hsp40) homologue, subfamily A,
     member 1; DNAJA1NM_001539
filamin B, beta (actin-binding protein 278); FLNBNM_001457
heat shock 70-kd protein 5; HSPA5NM_005347
heat shock 70-kd protein 9b; HSPA9BBC024034
protein phosphatase 1g (formerly 2c),
     magnesium-dependent, gamma isoform; PPM1GNM_002707
t complex–associated testis-expressed 1-like 1;
tetratricopeptide repeat domain 1; TCC1NM_0033114
thioredoxin-like 1; TXNL1AF052659
tubulin-specific chaperone c; TBCCBC020170
zinc finger–like protein 9; ZPR9AY046059
  • Yeast two-hybrid screening was carried using the pLexA system according to the protocol of Gyuris et al. (1993). For details see Supplementary materials and methods. Approximately 90% of the clones contained a sub-sequence of the ER-resident chaperone heat shock 70-kD protein 5 (HSPA5, grp-78), most probably reflecting the requirement of efficient folding of the VDAC1 protein in yeast. The results of sequencing of the remaining clones are shown in the table. One group of the putative interacting proteins were found to be cytoskeletal and signaling elements (shown in bold); another group (shown in normal) were found to be folding intermediates, presumably underlying the proper function of VDAC1.