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108. Meiosis-specific recombinase Dmc1 is a potent inhibitor of the Srs2 antirecombinase.

Author

Brooks Crickard, J., Kaniecki, Kyle, Kwon, Youngho, Sung, Patrick, and Greene, Eric C.

Subjects
MEIOSIS, CHROMOSOME analysis, GENETICS, SACCHAROMYCES cerevisiae, HYDROLYSIS
Abstract

Cross-over recombination products are a hallmark of meiosis because they are necessary for accurate chromosome segregation and they also allow for increased genetic diversity during sexual reproduction. However, cross-overs can also cause gross chromosomal rearrangements and are therefore normally down-regulated during mitotic growth. The mechanisms that enhance cross-over product formation upon entry into meiosis remain poorly understood. In Saccharomyces cerevisiae, the Superfamily 1 (Sf1) helicase Srs2, which is an ATP hydrolysis-dependent motor protein that actively dismantles recombination intermediates, promotes synthesisdependent strand annealing, the result of which is a reduction in cross-over recombination products. Here, we show that the meiosisspecific recombinase Dmc1 is a potent inhibitor of Srs2. Biochemical and single-molecule assays demonstrate that Dmc1 acts by inhibiting Srs2 ATP hydrolysis activity, which prevents the motor protein from undergoing ATP hydrolysis-dependent translocation on Dmc1- bound recombination intermediates. We propose a model in which Dmc1 helps contribute to cross-over formation during meiosis by antagonizing the antirecombinase activity of Srs2. [ABSTRACT FROM AUTHOR]

Published
2018
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113. Sequential eviction of crowded nucleoprotein complexes by the exonuclease RecBCD molecular motor.

Author

Tsuyoshi Terakawa, Redding, Sy, Silverstein, Timothy D., and Greene, Eric C.

Subjects
HELICASES, MOLECULAR motor proteins, NUCLEOPROTEINS, SINGLE molecules, DNA structure, DNA-binding proteins
Abstract

In physiological settings, all nucleic acids motor proteins must travel along substrates that are crowded with other proteins. However, the physical basis for how motor proteins behave in these highly crowded environments remains unknown. Here, we use real-time single-molecule imaging to determine how the ATP-dependent translocase RecBCD travels along DNA occupied by tandem arrays of high-affinity DNA binding proteins. We show that RecBCD forces each protein into its nearest adjacent neighbor, causing rapid disruption of the protein--nucleic acid interaction. This mechanism is not the same way that RecBCD disrupts isolated nucleoprotein complexes on otherwise naked DNA. Instead, molecular crowding itself completely alters the mechanism by which RecBCD removes tightly bound protein obstacles from DNA. [ABSTRACT FROM AUTHOR]

Published
2017
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123. A change of view: homologous recombination at single-molecule resolution

Author

Kaniecki, Kyle, De Tullio, Luisina, and Greene, Eric C.

Abstract

Genetic recombination occurs in all organisms and is vital for genome stability. Indeed, in humans, aberrant recombination can lead to diseases such as cancer. Our understanding of homologous recombination is built upon more than a century of scientific inquiry, but achieving a more complete picture using ensemble biochemical and genetic approaches is hampered by population heterogeneity and transient recombination intermediates. Recent advances in single-molecule and super-resolution microscopy methods help to overcome these limitations and have led to new and refined insights into recombination mechanisms, including a detailed understanding of DNA helicase function and synaptonemal complex structure. The ability to view cellular processes at single-molecule resolution promises to transform our understanding of recombination and related processes.

Published
2018
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