Structural heterogeneity of Pseudomonas aeruginosa bacterioferritin. 1994

G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
Centre for Metalloprotein Spectroscopy and Biology, School of Chemical, University of East Anglia, Norwich, U.K.

The subunit composition, amino acid sequence and haem-binding characteristics of bacterioferritin (BFR) from Pseudomonas aeruginosa have been studied. Unlike other BFRs, P. aeruginosa BFR was found to contain two subunit types, designated alpha and beta, which differed considerably in their amino acid sequences. The N-terminal 69 and 55 amino acids of the alpha and beta subunits respectively were determined. The alpha subunit differed most from other BFRs. The two subunits were present in variable proportions in different preparations. The maximum stoichiometry of haem binding was found to be sample-dependent and to be different from the previously reported one per subunit [Kadir and Moore (1990) FEBS Lett. 271, 141-143]. This previous haem-binding study was shown to have been carried out with damaged protein, which contained both normal alpha and beta subunits and shorter versions of these that appeared to have been produced by cleavage of the normal subunits. The possibility that aging processes degrade ferritins and affect their haem-binding characteristics is discussed.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011550 Pseudomonas aeruginosa A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection. Bacillus aeruginosus,Bacillus pyocyaneus,Bacterium aeruginosum,Bacterium pyocyaneum,Micrococcus pyocyaneus,Pseudomonas polycolor,Pseudomonas pyocyanea
D003573 Cytochrome b Group Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group. Cytochromes Type b,Cytochromes, Heme b,Group, Cytochrome b,Heme b Cytochromes,Type b, Cytochromes,b Cytochromes, Heme,b Group, Cytochrome
D005293 Ferritins Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types. Basic Isoferritin,Ferritin,Isoferritin,Isoferritin, Basic
D006418 Heme The color-furnishing portion of hemoglobin. It is found free in tissues and as the prosthetic group in many hemeproteins. Ferroprotoporphyrin,Protoheme,Haem,Heme b,Protoheme IX
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D017421 Sequence Analysis A multistage process that includes the determination of a sequence (protein, carbohydrate, etc.), its fragmentation and analysis, and the interpretation of the resulting sequence information. Sequence Determination,Analysis, Sequence,Determination, Sequence,Determinations, Sequence,Sequence Determinations,Analyses, Sequence,Sequence Analyses
D046911 Macromolecular Substances Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure. Macromolecular Complexes,Macromolecular Compounds,Macromolecular Compounds and Complexes,Complexes, Macromolecular,Compounds, Macromolecular,Substances, Macromolecular

Related Publications

G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
January 2018, PloS one,
G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
February 2010, Biochemistry,
G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
July 2022, Antibiotics (Basel, Switzerland),
G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
October 1975, European journal of biochemistry,
G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
August 1975, Infection and immunity,
G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
November 2020, Pathogens (Basel, Switzerland),
G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
January 1986, Journal of inorganic biochemistry,
G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
June 1999, Journal of bacteriology,
G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
January 2021, ACS infectious diseases,
G R Moore, and F H Kadir, and F K al-Massad, and N E Le Brun, and A J Thomson, and C Greenwood, and J N Keen, and J B Findlay
March 2020, ACS infectious diseases,
Copied contents to your clipboard!