The effect of the EAAEAE insert on the property of human metallothionein-3.
MT3 shows apparently different properties and function from MT1 even though they have 70% sequence homology. Possibly the two inserts, Thr5 and a negatively charged hexapeptide at position-55 in MT3, play important roles. A series of MT3 variants around the EAAEAE hexapeptide have been prepared by site-directed mutagenesis and their properties and reactivity towards pH, EDTA and DTNB have been studied. Our detailed studies revealed that the EAAEAE insert is essential to the property of MT3. It is the hexapeptide insert, to some extent, making the MT3 alpha-domain looser and lower stability of the metal-thiolate cluster, which could be accessed more easily.
Chemical Biology Laboratory, Department of Chemistry, Fudan University, Shanghai 200433.
Qi
Q
Zheng
Wan-Ming
WM
Yang
Wen-Hao
WH
Yu
Bin
B
Cai
Xin-Chen
XC
Teng
Yi
Y
Xie
Hong-Zhe
HZ
Sun
Ming-Jie
MJ
Zhang
Zhong-Xian
ZX
Huang
D004228:Dithionitrobenzoic Acid / Q000378:metabolism; D004492:Edetic Acid / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013058:Mass Spectrometry; D000090023:Metallothionein 3; D009154:Mutation; D009419:Nerve Tissue Proteins / Q000235:genetics* / Q000378:metabolism; D017384:Sequence Deletion
D000090023:Metallothionein 3; D009419:Nerve Tissue Proteins; D004228:Dithionitrobenzoic Acid; D004492:Edetic Acid