Genome-Based Analysis of Heme Biosynthesis and Uptake in Prokaryotic Systems

被引:43
作者
Cavallaro, Gabriele [1 ,2 ]
Decaria, Leonardo [1 ]
Rosato, Antonio [1 ,2 ]
机构
[1] Univ Florence, Magnet Resonance Ctr CERM, I-50019 Sesto Fiorentino, Italy
[2] Univ Florence, Dept Chem, I-50019 Sesto Fiorentino, Italy
关键词
heme; heme biosynthesis; heme uptake; NEAT domain; Peripla_BP_2 domain;
D O I
10.1021/pr8004309
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Heme is the prosthetic group of many proteins that carry out a variety of key biological functions. In addition, for many pathogenic organisms, heme (acquired from the host) may constitute a very important source of iron. Organisms can meet their heme demands by taking it up from external sources, by producing the cofactor through a dedicated biosynthetic pathway, or both. Here we analyzed the distribution of proteins specifically involved in the processes of heme biosynthesis and heme uptake in 474 prokaryotic organisms. These data allowed us to identify which organisms are capable of performing none, one, or both processes, based on the similarity to known systems. Some specific instances where one or more proteins along the pathways had unusual modifications were singled out. For two key protein domains involved in heme uptake, we could build a series of structural models, which suggested possible alternative modes of heme binding. Future directions for experimental work are given.
引用
收藏
页码:4946 / 4954
页数:9
相关论文
共 70 条
[1]  
Andrikopoulos Nikolaos K., 2002, Journal of Medicinal Food, V5, P1, DOI 10.1089/109662002753723160
[2]   Bis-methionyl coordination in the crystal structure of the heme-binding domain of the streptococcal cell surface protein shp [J].
Aranda, Roman ;
Worley, Chad E. ;
Liu, Mengyao ;
Bitto, Eduard ;
Cates, M. Susan ;
Olson, John S. ;
Lei, Benfang ;
Phillips, George N., Jr. .
JOURNAL OF MOLECULAR BIOLOGY, 2007, 374 (02) :374-383
[3]   The functions of Sco proteins from genome-based analysis [J].
Banci, Lucia ;
Bertini, Ivano ;
Cavallaro, Gabriele ;
Rosato, Antonio .
JOURNAL OF PROTEOME RESEARCH, 2007, 6 (04) :1568-1579
[4]  
Bateman A, 2002, NUCLEIC ACIDS RES, V30, P276, DOI [10.1093/nar/gkr1065, 10.1093/nar/gkp985, 10.1093/nar/gkh121]
[5]   Identification and characterization of a Streptococcus pyogenes operon involved in binding of hemoproteins and acquisition of iron [J].
Bates, CS ;
Montañez, GE ;
Woods, CR ;
Vincent, RM ;
Eichenbaum, Z .
INFECTION AND IMMUNITY, 2003, 71 (03) :1042-1055
[6]   Bioinorganic chemistry in the postgenomic era [J].
Bertini, I ;
Rosato, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2003, 100 (07) :3601-3604
[7]   Cytochrome c: Occurrence and functions [J].
Bertini, I ;
Cavallaro, G ;
Rosato, A .
CHEMICAL REVIEWS, 2006, 106 (01) :90-115
[8]   Evolution of mitochondrial-type cytochrome c domains and of the protein machinery for their assembly [J].
Bertini, Ivano ;
Cavallaro, Gabriele ;
Rosato, Antonio .
JOURNAL OF INORGANIC BIOCHEMISTRY, 2007, 101 (11-12) :1798-1811
[9]   Iron uptake mechanisms and their regulation in pathogenic bacteria [J].
Braun, V .
INTERNATIONAL JOURNAL OF MEDICAL MICROBIOLOGY, 2001, 291 (02) :67-79
[10]   A Streptococcus pneumoniae pathogenicity island encoding an ABC transporter involved in iron uptake and virulence [J].
Brown, JS ;
Gilliland, SM ;
Holden, DW .
MOLECULAR MICROBIOLOGY, 2001, 40 (03) :572-585