Two distinct ferritin-like molecules in Pseudomonas aeruginosa: the product of the bfrA gene is a bacterial ferritin (FtnA) and not a bacterioferritin (Bfr).
Two distinct ferritin-like molecules in Pseudomonas aeruginosa: the product of the bfrA gene is a bacterial ferritin (FtnA) and not a bacterioferritin (Bfr).
复制标题
DOI：
10.1021/bi2004119
复制
发表时间：
2011-06-14
期刊：
影响因子：
2.9
通讯作者：
Rivera M
中科院分区：
文献类型：
--
作者：
Yao H;Jepkorir G;Lovell S;Nama PV;Weeratunga S;Battaile KP;Rivera M
细菌中通常存在两种不同类型的类铁蛋白分子，即结合血红素的细菌铁蛋白(BfR)和非结合血红素的细菌铁蛋白(FTN)。从铜绿假单胞菌中早期分离的铁蛋白样分子表明，细菌铁蛋白可能是由两个不同的亚基组装而成的[Moore，G.R.，Kadir，F.H.，Al-Massad，F.K.，Le Brun，N.E.，Thomson，A.J.，Greenwood，C.，Keen，J.N.和Findlay，J.B.C.(1994)Biochem。J.304,493-497]。随后的研究证实在铜绿假单胞菌中存在两个编码类铁蛋白分子的基因，命名为bfrA和BFRB，并提示两种不同的细菌铁素可能共存[Ma，J.-F.，Ochsner，UA，Klotz，M.G，Nanayakkara，V.K.，Howell，M.L.，Johnson，Z.，Posey，J.E.，Vasil，M.L.，摩纳哥，J.J.，和Hassett，D.J.(1999)J.细菌素。181,3730-3742]。在这份报告中，我们提供了结构证据，证明bfrA基因的产物是一个铁蛋白样分子，不能结合血红素，它含有一个催化活性的铁氧酶中心，其结构性质类似于细菌和古生物Ftns的特征，而明显不同于典型的BFR铁氧基酶中心。因此，在铜绿假单胞菌中bfrA基因的产物是一种细菌铁蛋白，我们建议将其命名为PaFtnA。这些结果，加上之前BFRB基因产物是真正的细菌铁蛋白(PA BFRB)的特征[Weeratunga，S.J.，Lovell，S.，姚，H.，Battaile，K.P.，Fischer，C.J.，Gee，C.E.，和Rivera，M.(2010)生物化学49。1160-1175]表明铜绿假单胞菌中细菌铁蛋白(Pa FtnA)和细菌铁蛋白(Pa BFRB)共存。与这一观点一致，我们还获得了证据表明，Pa BFRB和Pa FtnA的铁释放可能受到铜绿假单胞菌不同的调控：而Pa FtnA中存储的铁的有效释放只需要铁还蛋白NADP还原酶(Pa Fpr)的电子输入，而存储在Pa BFRB中的铁的释放不仅需要Pa Ffr的电子传递，还需要“调节剂”的存在，这是细菌铁蛋白相关的铁氧还蛋白(Apo BFD)的存在形式。最后，对晶体中铁摄取的结构分析表明，铁氧合酶铁可能内化到Pa FtnA的内腔中。
Two distinct types of ferritin-like molecules often coexist in bacteria, the heme binding bacterioferritins (Bfr) and the non-heme binding bacterial ferritins (Ftn). The early isolation of a ferritin-like molecule from P. aeruginosa suggested the possibility of a bacterioferritin assembled from two different subunits [Moore, G. R., Kadir, F. H., Al-Massad, F. K., Le Brun, N. E., Thomson, A. J., Greenwood, C., Keen, J. N. and Findlay, J. B. C. (1994) Biochem. J. 304, 493–497]. Subsequent studies demonstrated the presence of two genes coding for ferritin-like molecules in P. aeruginosa, designated bfrA and bfrB, and suggested that two distinct bacterioferritins may coexist [Ma, J.-F., Ochsner, U. A., Klotz, M. G, Nanayakkara, V. K., Howell, M. L., Johnson, Z., Posey, J. E., Vasil, M. L., Monaco, J. J., and Hassett, D. J. (1999) J. Bacteriol. 181, 3730–3742]. In this report we present structural evidence demonstrating that the product of the bfrA gene is a ferritin-like molecule not capable of binding heme which harbors a catalytically active ferroxidase center with structural properties similar to those characteristic of bacterial and archaeal Ftns and clearly distinct from the ferroxidase center typical of Bfrs. Consequently, the product of the bfrA gene in P. aeruginosa is a bacterial ferritin, which we propose should be termed Pa FtnA. These results, together with the previous characterization of the product of the bfrB gene as a genuine bacterioferritin (Pa BfrB) [Weeratunga, S. J., Lovell, S., Yao, H., Battaile, K. P., Fischer, C. J., Gee, C. E., and Rivera, M. (2010) Biochemistry 49. 1160–1175] indicate the coexistence of a bacterial ferritin (Pa FtnA) and a bacterioferritin (Pa BfrB) in P. aeruginosa. In agreement with this idea, we also obtained evidence demonstrating that release of iron from Pa BfrB and Pa FtnA is likely subject to different regulation in P. aerugionsa: Whereas the efficient release of iron stored in Pa FtnA requires only the input of electrons from a ferredoxin NADP reductase (Pa Fpr), the release of iron stored in Pa BfrB requires not only electron delivery by Pa Fpr, but the presence of a “regulator”, the apo form of a bacterioferritin-associated ferredoxin (Pa apo Bfd). Finally, structural analysis of iron uptake in crystallo suggests a possible pathway for the internalization of ferroxidase iron into the interior cavity of Pa FtnA.
登录
查看更多内容
DOI：
10.1107/s0907444905036693
发表时间：
2006-01-01
影响因子：
2.2
作者：
Evans, P
通讯作者：
Evans, P
DOI：
10.1107/s0907444904019158
发表时间：
2004-12-01
影响因子：
2.2
作者：
Emsley, P;Cowtan, K
通讯作者：
Cowtan, K
DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH
影响因子：
3.2
作者：
ANDREWS, SC;HARRISON, PM;GUEST, JR
通讯作者：
GUEST, JR
DOI：
10.1002/prot.10286
发表时间：
2003-02-15
期刊：
PROTEINS-STRUCTURE FUNCTION AND GENETICS
影响因子：
--
作者：
Lovell, SC;Davis, IW;Richardson, DC
通讯作者：
Richardson, DC