Role of conserved histidine residues in metalloactivation of the ArsA ATPase

被引:10
作者
Bhattacharjee, H [1 ]
Rosen, BP [1 ]
机构
[1] Wayne State Univ, Sch Med, Dept Biochem & Mol Biol, Detroit, MI 48201 USA
关键词
ion-translocating ATPase; arsenite resistance; antimonite resistance; signal transduction pathway;
D O I
10.1023/A:1009200215328
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The ArsA ATPase is the catalytic subunit of a pump that is responsible for resistance to arsenicals and antimonials in Escherichia coli. Arsenite or antimonite allosterically activates the ArsA ATPase activity. ArsA homologues from eubacteria, archaea and eukarya have a signature sequence (DTAPTGHT) that includes a conserved histidine. The ArsA ATPase has two such conserved motifs, one in the NH2-terminal (A1) half and the other in the COOH-terminal (A2) half of the protein. These sequences have been proposed to be signal transduction domains that transmit the information of metal occupancy at the allosteric to the catalytic site to activate ATP hydrolysis. The role of the conserved residues His148 and His453, which reside in the A1 and A2 signal transduction domains respectively, was investigated by mutagenesis to create H148A, H453A or H148A/H453A ArsAs. Each altered protein exhibited a decrease in the V-max of metalloid-activated ATP hydrolysis, in the order wild type ArsA > H148A > H453A > H148A/H453A. These results suggest that the histidine residues play a role in transmission of the signal between the catalytic and allosteric sites.
引用
收藏
页码:281 / 288
页数:8
相关论文
共 17 条
[1]  
Bhattacharjee H, 1999, SYMP SOC GEN MICROBI, V58, P58
[2]   Spatial proximity of Cys(113), Cys(172), and Cys(422) in the metalloactivation domain of the ArsA ATPase [J].
Bhattacharjee, H ;
Rosen, BP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (40) :24465-24470
[3]   ROLE OF CYSTEINYL RESIDUES IN METALLOACTIVATION OF THE OXYANION-TRANSLOCATING ARSA ATPASE [J].
BHATTACHARJEE, H ;
LI, JX ;
KSENZENKO, MY ;
ROSEN, BP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (19) :11245-11250
[4]  
HSU CM, 1989, J BIOL CHEM, V264, P17349
[5]  
KARKARIA CE, 1990, J BIOL CHEM, V265, P7832
[6]  
KAUR P, 1992, J BIOL CHEM, V267, P19272
[7]   The linker peptide of the ArsA ATPase [J].
Li, JX ;
Rosen, BP .
MOLECULAR MICROBIOLOGY, 2000, 35 (02) :361-367
[8]  
Mukhopadhyay R, 1998, ADV EXP MED BIOL, V456, P159
[9]   Nucleotide binding to the C-terminal nucleotide binding domain of ArsA -: Studies with an ATP analogue, 5′-p-fluorosulfonylbenzoyladenosine (FSBA) [J].
Ramaswamy, S ;
Kaur, P .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (15) :9243-9248
[10]   Mechanism of the ArsA ATPase [J].
Rosen, BP ;
Bhattacharjee, H ;
Zhou, TQ ;
Walmsley, AR .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 1999, 1461 (02) :207-215