TY - JOUR
T1 - A biological function for cadmium in marine diatoms
AU - Lane, Todd W.
AU - Morel, Francois M. M.
PY - 2000/4/25
Y1 - 2000/4/25
N2 - The oceanic distribution of cadmium follows closely that of major algal nutrients such as phosphate. The reasons for this 'nutrient-like' distribution are unclear, however, because cadmium is not generally believed to have a biological function. Herein, we provide evidence of a biological role for Cd in the marine diatom Thalassiosira weissflogii under conditions of low zinc, typical of the marine environment. Addition of Cd to Zn-limited cultures enhances the growth rate of T. weissflogii, particularly at low pCO2. This increase in growth rate is reflected in increased levels of cellular carbonic anhydrase (CA) activity, although the levels of TWCA1, the major intracellular Zn-requiring isoform of CA in T(r) weissflogii, remain low. 109Cd label comigrates with a protein band that shows CA activity and is distinct from TWCA1 on native PAGE of radiolabeled T. weissflogii cell lysates. The levels of the Cd protein are modulated by CO2 in a manner that is consistent with a role for this enzyme in carbon acquisition. Purification of the CA-active fraction leads to the isolation of a Cd-containing protein of 43 kDa. It is now clear that T. weissflogii expresses a Cd-specific CA, which, particularly under conditions of Zn limitation, can replace the Zn enzyme TWCA1 in its carbon-concentrating mechanism.
AB - The oceanic distribution of cadmium follows closely that of major algal nutrients such as phosphate. The reasons for this 'nutrient-like' distribution are unclear, however, because cadmium is not generally believed to have a biological function. Herein, we provide evidence of a biological role for Cd in the marine diatom Thalassiosira weissflogii under conditions of low zinc, typical of the marine environment. Addition of Cd to Zn-limited cultures enhances the growth rate of T. weissflogii, particularly at low pCO2. This increase in growth rate is reflected in increased levels of cellular carbonic anhydrase (CA) activity, although the levels of TWCA1, the major intracellular Zn-requiring isoform of CA in T(r) weissflogii, remain low. 109Cd label comigrates with a protein band that shows CA activity and is distinct from TWCA1 on native PAGE of radiolabeled T. weissflogii cell lysates. The levels of the Cd protein are modulated by CO2 in a manner that is consistent with a role for this enzyme in carbon acquisition. Purification of the CA-active fraction leads to the isolation of a Cd-containing protein of 43 kDa. It is now clear that T. weissflogii expresses a Cd-specific CA, which, particularly under conditions of Zn limitation, can replace the Zn enzyme TWCA1 in its carbon-concentrating mechanism.
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U2 - 10.1073/pnas.090091397
DO - 10.1073/pnas.090091397
M3 - Article
C2 - 10781068
AN - SCOPUS:0034712970
SN - 0027-8424
VL - 97
SP - 4627
EP - 4631
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 9
ER -