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      ABC transporter research: going strong 40 years on

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          Abstract

          In most organisms, ABC transporters constitute one of the largest families of membrane proteins. In humans, their functions are diverse and underpin numerous key physiological processes, as well as being causative factors in a number of clinically relevant pathologies. Advances in our understanding of these diseases have come about through combinations of genetic and protein biochemical investigations of these transporters and the power of in vitro and in vivo investigations is helping to develop genotype–phenotype understanding. However, the importance of ABC transporter research goes far beyond human biology; microbial ABC transporters are of great interest in terms of understanding virulence and drug resistance and industrial biotechnology researchers are exploring the potential of prokaryotic ABC exporters to increase the capacity of synthetic biology systems. Plant ABC transporters play important roles in transport of hormones, xenobiotics, metals and secondary metabolites, pathogen responses and numerous aspects of development, all of which are important in the global food security area. For 3 days in Chester, this Biochemical Society Focused Meeting brought together researchers with diverse experimental approaches and with different fundamental questions, all of which are linked by the commonality of ABC transporters.

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          Most cited references59

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          Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold.

          The alpha- and beta-subunits of membrane-bound ATP synthase complex bind ATP and ADP: beta contributes to catalytic sites, and alpha may be involved in regulation of ATP synthase activity. The sequences of beta-subunits are highly conserved in Escherichia coli and bovine mitochondria. Also alpha and beta are weakly homologous to each other throughout most of their amino acid sequences, suggesting that they have common functions in catalysis. Related sequences in both alpha and beta and in other enzymes that bind ATP or ADP in catalysis, notably myosin, phosphofructokinase, and adenylate kinase, help to identify regions contributing to an adenine nucleotide binding fold in both ATP synthase subunits.
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            Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA.

            Overlapping complementary DNA clones were isolated from epithelial cell libraries with a genomic DNA segment containing a portion of the putative cystic fibrosis (CF) locus, which is on chromosome 7. Transcripts, approximately 6500 nucleotides in size, were detectable in the tissues affected in patients with CF. The predicted protein consists of two similar motifs, each with (i) a domain having properties consistent with membrane association and (ii) a domain believed to be involved in ATP (adenosine triphosphate) binding. A deletion of three base pairs that results in the omission of a phenylalanine residue at the center of the first predicted nucleotide-binding domain was detected in CF patients.
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              Plant ABC proteins--a unified nomenclature and updated inventory.

              The ABC superfamily comprises both membrane-bound transporters and soluble proteins involved in a broad range of processes, many of which are of considerable agricultural, biotechnological and medical potential. Completion of the Arabidopsis and rice genome sequences has revealed a particularly large and diverse complement of plant ABC proteins in comparison with other organisms. Forward and reverse genetics, together with heterologous expression, have uncovered many novel roles for plant ABC proteins, but this progress has been accompanied by a confusing proliferation of names for plant ABC genes and their products. A consolidated nomenclature will provide much-needed clarity and a framework for future research.
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                Author and article information

                Journal
                Biochem Soc Trans
                Biochem. Soc. Trans
                ppbiost
                BST
                Biochemical Society Transactions
                Portland Press Ltd.
                0300-5127
                1470-8752
                9 October 2015
                1 October 2015
                : 43
                : 5 ( displayID: 5 )
                : 1033-1040
                Affiliations
                [* ]Biological Chemistry and Crop Protection Department, Rothamsted Research, Harpenden, AL5 2JQ, U.K.
                []School of Life Sciences, Queen's Medical Centre, University of Nottingham, Nottingham, NG7 2UH, U.K.
                Author notes
                1Correspondence may be addressed to either author (email freddie.theodoulou@ 123456rothamsted.ac.uk or ian.kerr@ 123456nottingham.ac.uk ).
                Article
                BST20150139
                10.1042/BST20150139
                4652935
                26517919
                9c8cdf46-6af5-48e1-88fa-1153e2206cb6
                © 2015 Authors

                This is an open access article published by Portland Press Limited and distributed under the Creative Commons Attribution Licence 3.0.

                History
                : 3 June 2015
                Page count
                Figures: 2, Tables: 1, References: 62, Pages: 8
                Categories
                Biochemical Society Focused Meetings
                ATP binding cassette transporters: from mechanism to organism
                ATP binding cassette transporters: from mechanism to organism
                S7

                Biochemistry
                atp-binding cassette (abc) transporter,disease,multi-drug resistance,protein structure,transport mechanism

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