SufS protein from Haloferax volcanii involved in Fe-S cluster assembly in haloarchaea.
NifS-like proteins are pyridoxal 5'-phosphate (PLP)-dependent enzymes involved in sulphur transfer metabolism. These enzymes have been catalogued as cysteine desulphurases (CDs) which catalyse the conversion of L-cysteine into L-alanine and an enzyme-bound persulphide radical. This reaction, assisted by different scaffold protein machineries, seems to be the main source of sulphur for the synthesis of essential cofactors of the [Fe-S] cluster. CDs genes have been detected in the tree domains of life, but, up until now, there has been no biochemical characterisation or study into the physiological role of this enzyme in haloarchaea. In this study, we have cloned, expressed and characterised a cysteine desulphurase (SufS) from Haloferax volcanii and demonstrated that this protein is able to reconstitute the [Fe-S] cluster of halophilic ferredoxin.
División de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Alicante, Ap. 99, E-03080 Alicante, Spain. basilio.zafrilla@ua.es
Basilio
B
Zafrilla
Rosa María
RM
Martínez-Espinosa
Julia
J
Esclapez
Francisco
F
Pérez-Pomares
María José
MJ
Bonete
D001105:Archaea / Q000378:metabolism*; D017931:DNA Primers / Q000737:chemistry; D030562:Databases, Protein; D004305:Dose-Response Relationship, Drug; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D019621:Haloferax / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007506:Iron-Sulfur Proteins / Q000737:chemistry*; D008190:Lyases / Q000235:genetics* / Q000378:metabolism*; D009711:Nucleotides / Q000737:chemistry; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D014466:Ultraviolet Rays
D017931:DNA Primers; D007506:Iron-Sulfur Proteins; D009711:Nucleotides; D011994:Recombinant Proteins; D008190:Lyases; C034278:selenocysteine lyase