Isolation and preliminary characterization of a Cd-binding protein from Tenebrio molitor (Coleoptera).
The effect of cadmium (Cd) exposure on Cd-binding ligands was investigated for the first time in a beetle (Coleoptera), using the mealworm Tenebrio molitor (L) as a model species. Exposure to Cd resulted in an approximate doubling of the Cd-binding capacity of the protein extracts from whole animals. Analysis showed that the increase was mainly explained by the induction of a Cd-binding protein of 7134.5 Da, with non-metallothionein characteristics. Amino acid analysis and de novo sequencing revealed that the protein has an unusually high content of the acidic amino acids aspartic and glutamic acid that may explain how this protein can bind Cd even without cysteine residues. Similarities in the amino acid composition suggest it to belong to a group of little studied proteins often referred to as "Cd-binding proteins without high cysteine content". This is the first report on isolation and peptide sequence determination of such a protein from a coleopteran.
Pedersen
S A
SA
Department of Biology, Realfagsbygget, Norwegian University of Science and Technology (NTNU), N-7491 Trondheim, Norway. sindre.pedersen@bio.ntnu.no
Kristiansen
E
E
Andersen
R A
RA
Zachariassen
K E
KE
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D003545:Cysteine / Q000032:analysis; D013058:Mass Spectrometry; D008668:Metallothionein / Q000032:analysis / Q000737:chemistry / Q000302:isolation & purification*; D008970:Molecular Weight; D013712:Tenebrio / Q000737:chemistry*
D000596:Amino Acids; C004203:cadmium-binding protein; D008668:Metallothionein; D003545:Cysteine