File:PICH and BLM dependant DNA catenation resolution model.jpg
PICH_and_BLM_dependant_DNA_catenation_resolution_model.jpg (643 × 380 pixels, file size: 108 KB, MIME type: image/jpeg)
Title: Model for ultrafine anaphase bridge PICH/BLM dependant decatenation
Comment: The model for ultrafine anaphase bridge decatenation, which is dependant on BLM/PICH proteins which allow for the topoisomerase IIa to bind and cut the DNA. If topo IIa does not carry out its job successfully, centromeric nondisjunction may result, as well as the creation of more ultrafine anaphase bridges.
Original figure legend: Model of PICH/BLM-dependent decatenation of centromeric DNA.
Copyright Rouzeau et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Original image file name: pone.0033905.g006
Web address: http://www.ncbi.nlm.nih.gov/pubmed/22563370
Paper title: Bloom's syndrome and PICH helicases cooperate with topoisomerase IIα in centromere disjunction before anaphase.
Figure legend: We propose that the combined action of BLM and PICH promotes the organization of centromeric chromatin, thereby rendering some centromeric catenates accessible to Topo IIα. In the absence of BLM or PICH, a defect in the recruitment of active Topo IIα results in the persistence of some catenations leading to centromeric non disjunction and the formation of additional UFBs.
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|current||11:42, 16 May 2013||643 × 380 (108 KB)||Z3375878||The model for ultrafine anaphase bridge decatenation, which is dependant on BLM/PICH proteins which allow for the topoisomerase IIa to bind and cut the DNA. If topo IIa does not carry out its job successfully, centromeric nondisjunction may result, as ...|