Bacterial zinc uptake and regulators

被引:249
作者
Hantke, K [1 ]
机构
[1] Univ Tubingen, D-72076 Tubingen, Germany
关键词
D O I
10.1016/j.mib.2005.02.001
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Many bacteria use an ABC transporter for high-affinity uptake of zinc with a cluster 9 solute-binding protein. Other members of this protein family transport manganese. At present, it is not always possible to distinguish zinc-specific and manganese-specific transporters on the basis of sequence analysis. Low-affinity ZIP-type zinc transporters in bacteria have also been identified. Most high-affinity zinc uptake systems are regulated by Zur proteins, which form at least three unrelated subgroups of the Fur protein family (regulators of iron transport). High-affinity transport of zinc out of the periplasmic space poses a problem to the cell because zinc is a cofactor of several periplasmic enzymes. Certain zinc-binding proteins in the periplasm might function as chaperones to supply these enzymes with zinc.
引用
收藏
页码:196 / 202
页数:7
相关论文
共 28 条
[11]   The high-affinity zinc-uptake system znuA CB is under control of the iron-uptake regulator (fur) gene in the animal pathogen Pasteurella multocida [J].
Garrido, ME ;
Bosch, M ;
Medina, R ;
Llagostera, M ;
de Rozas, AMP ;
Badiola, I ;
Barbé, J .
FEMS MICROBIOLOGY LETTERS, 2003, 221 (01) :31-37
[12]   The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition [J].
Goetz, DH ;
Holmes, MA ;
Borregaard, N ;
Bluhm, ME ;
Raymond, KN ;
Strong, RK .
MOLECULAR CELL, 2002, 10 (05) :1033-1043
[13]   ZupT is a Zn(II) uptake system in Escherichia coli [J].
Grass, G ;
Wong, MD ;
Rosen, BP ;
Smith, RL ;
Rensing, C .
JOURNAL OF BACTERIOLOGY, 2002, 184 (03) :864-866
[14]   Bacterial zinc transporters and regulators [J].
Hantke, K .
BIOMETALS, 2001, 14 (3-4) :239-249
[15]   The Treponema pallidum tro operon encodes a multiple metal transporter, a zinc-dependent transcriptional repressor, and a semi-autonomously expressed phosphoglycerate mutase [J].
Hazlett, KRO ;
Rusnak, F ;
Kehres, DG ;
Bearden, SW ;
La Vake, CJ ;
La Vake, ME ;
Maguire, ME ;
Perry, RD ;
Radolf, JD .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (23) :20687-20694
[16]   The crystal structure of pneumococcal surface antigen PsaA reveals a metal-binding site and a novel structure for a putative ABC-type binding protein [J].
Lawrence, MC ;
Pilling, PA ;
Epa, VC ;
Berry, AM ;
Ogunniyi, AD ;
Paton, JC .
STRUCTURE, 1998, 6 (12) :1553-1561
[17]   The crystal structure of Zn(II)-free Treponema pallidum TroA, a periplasmic metal-binding protein, reveals a closed conformation [J].
Lee, YH ;
Dorwart, MR ;
Hazlett, KRO ;
Deka, RK ;
Norgard, MV ;
Radolf, JD ;
Hasemann, CA .
JOURNAL OF BACTERIOLOGY, 2002, 184 (08) :2300-2304
[18]  
MAKAROVA KS, 2001, GENOME BIOL, V2
[19]   The Mycobacterium tuberculosis Rv2358-furB operon is induced by zinc [J].
Milano, A ;
Branzoni, M ;
Canneva, F ;
Profumo, A ;
Riccardi, G .
RESEARCH IN MICROBIOLOGY, 2004, 155 (03) :192-200
[20]   Zinc is a key factor in controlling alternation of two types of L31 protein in the Bacillus subtilis ribosome [J].
Nanamiya, H ;
Akanuma, G ;
Natori, Y ;
Murayama, R ;
Kosono, S ;
Kudo, T ;
Kobayashi, K ;
Ogasawara, N ;
Park, SM ;
Ochi, K ;
Kawamura, F .
MOLECULAR MICROBIOLOGY, 2004, 52 (01) :273-283