Titlebook: SMC Complexes; Methods and Protocol Anjana Badrinarayanan Book 2019 Springer Science+Business Media, LLC, part of Springer Nature 2019 Chro

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In Vivo and In Vitro Assay for Monitoring the Topological Loading of Bacterial Condensins on DNAnsins to DNA. In addition, isolation of bacterial condensin and DNA complexes prevents any undesired interaction between them due to cross-linking reagents. These methodologies provide reproducible and reliable results for the loading of topologically bound proteins such as bacterial condensins.

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Analysis of the Chromosomal Localization of Yeast SMC Complexes by Chromatin ImmunoprecipitationhIP). Combined with the recent technological advancement in next generation sequencing, the ChIP assay can map the exact binding sites of a protein of interest across the entire genome. Here we describe a-step-by step protocol for ChIP followed by library preparation for ChIP-seq from yeast cells.

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Dissecting DNA Compaction by the Bacterial Condensin MukBnsins are well studied, the mechanism of the overall process executed by condensins, DNA compaction, remains unclear. Here, we describe some of the methods used routinely in our laboratory to understand the mechanism of DNA compaction by . condensin MukB.

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Identifying Functional Domains in Subunits of Structural Maintenance of Chromosomes (SMC) Complexes s called cohesin, condensin, and SMC5/6, which share the same basic architecture. The core of SMC complexes contains a heterodimer of SMC proteins, a kleisin subunit, and a set of regulatory proteins that contain HEAT and Armadillo (ARM) repeat protein–protein interaction motifs. A major challenge i

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Multicomponent Yeast Two-Hybrid System: Applications to Study Protein–Protein Interactions in SMC Co (SMC) complexes. SMC complexes are composed of SMC proteins, kleisin, and kleisin-interacting subunits. These subunits interact in specific ways to constitute and regulate the closed structure of the complexes. Specifically, kleisin molecules bridge the SMC dimers and the kleisin-interacting subuni