ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains

Schneider, Erwin

doi:10.1016/s0168-6445(98)00002-3

Cited by 122 publications

(159 citation statements)

References 91 publications

(164 reference statements)

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“…Assuming that Rad50's ATP binding is required for chromatin association, we postulate that the rad50-14 mutation causes the ATPase motif to become stuck in an ATP-bound conformation and that this allows both association of the MRN complex with chromatin and partial DSB processing (Acharya et al 2008), but inhibits detachment of the MRN complex from chromatin, by preventing ATP hydrolysis. This hypothesis corresponds with results by others that have shown that mutations in the conserved Walker B motif aspartate residue abolish ATP hydrolysis but may or may not disrupt ATP binding (Frelet and Klein 2006;Koronakis et al 1995;Panagiotidis et al 1993;Schneider and Hunke 1998;Shyamala et al 1991).…”

Section: Immunolocalizationsupporting

confidence: 90%

Meiotic localization of Mre11 and Rad50 in wild type, spo11-1, and MRN complex mutants of Coprinus cinereus

et al. 2009

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The Mre11-Rad50-Nbs1 (MRN) complex is required for numerous cellular processes that involve interactions with DNA double-strand breaks. For the majority of these processes, the MRN complex is thought to act as a unit, with each protein aiding the activity of the others. We have examined the relationship between Mre11 and Rad50 during meiosis in the basidiomycete Coprinus cinereus (Coprinopsis cinerea), investigating to what extent activities of Mre11 and Rad50 are interdependent. We showed that mre11-1 is epistatic to rad50-1 with respect to the time of meiotic arrest, indicating that Mre11 activity facilitates the diffuse diplotene arrest of rad50 mutants. Anti-Mre11 and anti-Rad50 antibodies were used to examine MRN complex localization in a wild-type strain and in spo11, mre11, and rad50 mutants. In wild type, numbers of Mre11 and Rad50 foci peaked at time points corresponding to leptotene and early zygotene. In the spo11-1 mutant, which is defective in meiotic double-strand break formation, foci accumulated throughout prophase I. Of seven MRN mutants examined, only two rad50 strains exhibited Mre11 and Rad50 foci that localized to chromatin, although Mre11 protein was found in the cell for all of them. Analysis of predicted mutant structures showed that stable localization of Mre11 and Rad50 does not depend upon a wild-type hook-proximal coiled coil, but does require the presence of the Rad50 ATPase/adenylate cyclase domains. We found that Mre11 and Rad50 were interdependent for binding to meiotic chromosomes. However, the majority of foci observed apparently contained only one of the two proteins. Independent Mre11 and Rad50 foci might indicate disassociation of the complex during meiosis or could reflect independent structural roles for the two proteins in meiotic chromatin.

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Section: Immunolocalizationsupporting

confidence: 90%

Meiotic localization of Mre11 and Rad50 in wild type, spo11-1, and MRN complex mutants of Coprinus cinereus

et al. 2009

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“…This region is known collectively as the H-loop [44] and corresponds approximately to a region earlier referred to as the switch region [7]. Comparison of the Xray structures of ABC NBDs reveals that the position of the histidine, and of the immediately downstream helix 7, is quite variable with respect to the central b sheet of the nucleotide-binding core, with this region appearing to pivot about Ca atoms at its N-and C-termini, a notion supported by our MD simulations of HisP, which reveal hinges at these points [55].…”

Section: What Is the Role Of The Conserved Active Site Histidine?mentioning

confidence: 99%

The ABC transporter structure and mechanism: perspectives on recent research

Jones

George

2004

Cellular and Molecular Life Sciences (CMLS)

509

366

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ATP-binding cassette (ABC) transporters are multidomain integral membrane proteins that utilise the energy of ATP hydrolysis to translocate solutes across cellular membranes in all phyla. ABC transporters form one of the largest of all protein families and are central to many important biomedical phenomena, including resistance of cancers and pathogenic microbes to drugs. Elucidation of the structure and mechanism of ABC transporters is essential to the rational design of agents to control their function. While a wealth of high-resolution structures of ABC proteins have been produced in recent years, many fundamental questions regarding the protein's mechanism remain unanswered. In this review, we examine the recent structural data concerning ABC transporters and related proteins in the light of other experimental and theoretical data, and discuss these data in relation to current ideas concerning the transporters' molecular mechanism.

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“…The ATP-binding cassette (ABC) superfamily comprises systems sharing common characteristics (Schneider and Hunke 1998). ABC systems are present in prokaryotes and in eukaryotes.…”

Section: Introductionmentioning

confidence: 99%

“…These were identified by comparing the predicted secondary structure of some ABC modules to the known three-dimensional structure of ATPhydrolyzing enzymes. These are the Switch region, named by analogy to a sequence in the RecA protein that was proposed to play a role in the propagation of conformational changes triggered by ATP hydrolysis, and some residues distal to the Switch region for which little functional information is available (Mourez et al 1997;Schneider and Hunke 1998).…”

Section: Introductionmentioning

confidence: 99%

Getting In or Out: Early Segregation Between Importers and Exporters in the Evolution of ATP-Binding Cassette (ABC) Transporters

1999

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ATP-binding cassette (ABC) systems, also called traffic ATPases, are found in eukaryotes and prokaryotes and almost all participate in the transport of a wide variety of molecules. ABC systems are characterized by a highly conserved ATPase module called here the ABC module, involved in coupling transport to ATP hydrolysis. We have used the sequence of one of the first representatives of bacterial ABC transporters, the MalK protein, to collect 250 closely related sequences from a nonredundant protein sequence database. The sequences collected by this objective method are all known or putative ABC transporters. After having eliminated short protein sequences and duplicates, the 197 remaining sequences were subjected to a phylogenetic analysis based on a mutational similarity matrix. An unrooted tree for these modules was found to display two major branches, one grouping all collected uptake systems and the other all collected export systems. This remarkable disposition strongly suggests that the divergence between these two functionally different types of ABC systems occurred once in the history of these systems and probably before the differentiation of prokaryotes and eukaryotes. We discuss the implications of this finding and we propose a model accounting for the generation and the diversification of ABC systems.

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ATP-binding-cassette (ABC) transport systems: Functional and structural aspects of the ATP-hydrolyzing subunits/domains

Cited by 122 publications

References 91 publications

Meiotic localization of Mre11 and Rad50 in wild type, spo11-1, and MRN complex mutants of Coprinus cinereus

Meiotic localization of Mre11 and Rad50 in wild type, spo11-1, and MRN complex mutants of Coprinus cinereus

The ABC transporter structure and mechanism: perspectives on recent research

Getting In or Out: Early Segregation Between Importers and Exporters in the Evolution of ATP-Binding Cassette (ABC) Transporters

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