Abstract
The Arabidopsis SHEPHERD (SHD) protein is an Hsp90-like molecular chaperone resident in the endoplasmic reticulum, however, its target protein has not yet been revealed. The shd-1 mutant in Ws strain shows clavata (clv)-like phenotype, in which carpel number is increased. Therefore, we presumed that CLV2 in Ws strain (CLV2Ws) required the SHD chaperoning activity for its function. In other words, we supposed CLV2Ws was the direct target of SHD.
To verify this prediction, we tried to confirm the direct binding between CLV2Ws and SHD. We detected it by pull-down assay and the surface plasmon resonance technique (Biacore system). Moreover, we also detected the binding between SHD and CLV2Col.
The shd mutant shows pleiotropic phenotypes, such as retarded root growth and inhibited pollen tube elongation. Therefore it indicates that SHD has other targets. So we performed LC-MS/MS analysis to investigate other targets of SHD.
