Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures

Hopfner, Karl‐Peter

doi:10.1016/s0959-440x(03)00037-x

Cited by 195 publications

(183 citation statements)

References 55 publications

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“…Mutation of the conserved Q-loop (Q147L) is predicted to block binding of the attacking nucleophile (water) and Mg 2ϩ ions involved in ATP hydrolysis (Hopfner et al, 2000). It has been suggested that contacts between the Q-loop glutamine, and the active site magnesium and nucleophile make it a good candidate for the transmission of allosteric changes caused by substrate binding (Hopfner and Tainer, 2003). However, no SMC Q-loop mutant has been characterized in vivo in detail to date.…”

Section: Atp Binding and Hydrolysis Are Required For Smc2 Functionmentioning

confidence: 99%

“…This motif has been proposed to bind water and magnesium and to undergo a conformational change upon substrate binding (Hopfner et al, 2000;Hopfner and Tainer, 2003). It has been suggested that this acts as a "lever arm" to transduce ATP binding and hydrolysis into physical action by the SMC protein (Hopfner and Tainer, 2003).…”

Section: Mechanistic Differences Between Cohesin and Condensin Atpasementioning

confidence: 99%

“…ATP binding through the signature and Q-loop motifs causes conformational changes necessary to accomplish functions as diverse as DNA repair and transmembrane transport (Hopfner and Tainer, 2003). Although several studies indicate that ATPase activity of condensin is needed for its enzymatic properties, the precise role of ATP binding and hydrolysis is not yet known.…”

Section: Introductionmentioning

confidence: 99%

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Molecular and Genetic Analysis of Condensin Function in Vertebrate Cells

Hudson

Ohta

Freisinger

et al. 2008

MBoC

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We engineered mutants into residues of SMC2 to dissect the role of ATPase function in the condensin complex. These residues are predicted to be involved in ATP binding or hydrolysis and in the Q-loop, which is thought to act as a mediator of conformational changes induced by substrate binding. All the engineered ATPase mutations resulted in lethality when introduced into SMC2 null cells. We found that ATP binding, but not hydrolysis, is essential to allow stable condensin association with chromosomes. How SMC proteins bind and interact with DNA is still a major question. Cohesin may form a ring structure that topologically encircles DNA. We examined whether condensin behaves in an analogous way to its cohesin counterpart, and we have generated a cleavable form of biologically active condensin with PreScission protease sites engineered into the SMC2 protein. This has allowed us to demonstrate that topological integrity of the SMC2-SMC4 heterodimer is not necessary for the stability of the condensin complex in vitro or for its stable association with mitotic chromosomes. Thus, despite their similar molecular organization, condensin and cohesin exhibit fundamental differences in their structure and function.

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Section: Atp Binding and Hydrolysis Are Required For Smc2 Functionmentioning

confidence: 99%

Section: Mechanistic Differences Between Cohesin and Condensin Atpasementioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Molecular and Genetic Analysis of Condensin Function in Vertebrate Cells

Hudson

Ohta

Freisinger

et al. 2008

MBoC

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“…In ABC transporters, energy from ATP binding/hydrolysis acts to transport specific substances across membranes (1)(2)(3)(4)(5)25). In soluble SMC proteins, the ABC ATPase utilizes ATP to recognize and bind DNA (4,26).…”

mentioning

confidence: 99%

Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis

Hirabayashi

Yuda

Tanaka

et al. 2015

Journal of Biological Chemistry

100

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ATP-binding cassette (ABC)-typeATPases are chemomechanical engines involved in diverse biological pathways. Recent genomic information reveals that ABC ATPase domains/subunits act not only in ABC transporters and structural maintenance of chromosome proteins, but also in iron-sulfur (Fe-S) cluster biogenesis. A novel type of ABC protein, the SufBCD complex, functions in the biosynthesis of nascent Fe-S clusters in almost all Eubacteria and Archaea, as well as eukaryotic chloroplasts. In this study, we determined the first crystal structure of the Escherichia coli SufBCD complex, which exhibits the common architecture of ABC proteins: two ABC ATPase components (SufC) with function-specific components (SufB-SufD protomers). Biochemical and physiological analyses based on this structure provided critical insights into Fe-S cluster assembly and revealed a dynamic conformational change driven by ABC ATPase activity. We propose a molecular mechanism for the biogenesis of the Fe-S cluster in the SufBCD complex.

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“…It belongs to the family of ATP-binding cassette (ABC) transporter proteins, which carry out a broad range of functions mainly in translocation of substrates across membranes, but are also involved in translation, DNA repair and chromosome maintenance. 1,2 In contrast to most ABC proteins, ABCE1 lacks the transmembrane domains and therefore is unlikely to participate in membrane transport. 3 ABC proteins typically contain twin nucleotide-binding domains (NBDs) that act as molecular engines coupling ATP hydrolysis to conformational changes in their substrate-binding sites.…”

Section: Introductionmentioning

confidence: 99%

ABCE1 is essential for S phase progression in human cells

et al. 2016

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ABCE1 is a highly conserved protein universally present in eukaryotes and archaea, which is crucial for the viability of different organisms. First identified as RNase L inhibitor, ABCE1 is currently recognized as an essential translation factor involved in several stages of eukaryotic translation and ribosome biogenesis. The nature of vital functions of ABCE1, however, remains unexplained. Here, we study the role of ABCE1 in human cell proliferation and its possible connection to translation. We show that ABCE1 depletion by siRNA results in a decreased rate of cell growth due to accumulation of cells in S phase, which is accompanied by inefficient DNA synthesis and reduced histone mRNA and protein levels. We infer that in addition to the role in general translation, ABCE1 is involved in histone biosynthesis and DNA replication and therefore is essential for normal S phase progression. In addition, we analyze whether ABCE1 is implicated in transcript-specific translation via its association with the eIF3 complex subunits known to control the synthesis of cell proliferation-related proteins. The expression levels of a few such targets regulated by eIF3A, however, were not consistently affected by ABCE1 depletion.

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Rad50/SMC proteins and ABC transporters: unifying concepts from high-resolution structures

Cited by 195 publications

References 55 publications

Molecular and Genetic Analysis of Condensin Function in Vertebrate Cells

Molecular and Genetic Analysis of Condensin Function in Vertebrate Cells

Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis

ABCE1 is essential for S phase progression in human cells

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