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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

RMI1, RecQ mediated genome instability 1, homolog

RMI1, BLAP75, RmII, NCE4
RMI1 is a component of protein complexes that limit DNA crossover formation via the dissolution of double Holliday junctions (Raynard et al., 2006 [PubMed 16595695]).[supplied by OMIM, Mar 2008] (from NCBI)
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Top mentioned proteins: Blm, CAN, Eme1, V1a, RPA
Papers on RMI1
Resolution of Recombination Intermediates: Mechanisms and Regulation.
Review
New
Wyatt et al., United Kingdom. In Cold Spring Harb Symp Quant Biol, Oct 2015
These involve (1) BLM-Topoisomerase IIIα-RMI1-RMI2 (BTR complex), (2) SLX1-SLX4-MUS81-EME1 (SLX-MUS complex), and (3) GEN1.
System-wide Analysis of SUMOylation Dynamics in Response to Replication Stress Reveals Novel Small Ubiquitin-like Modified Target Proteins and Acceptor Lysines Relevant for Genome Stability.
New
Vertegaal et al., Leiden, Netherlands. In Mol Cell Proteomics, May 2015
A large subset of these identified proteins function in one network that consists of interacting replication factors, transcriptional regulators, DNA damage response factors including MDC1, ATR-interacting protein ATRIP, the Bloom syndrome protein and the BLM-binding partner RMI1, the crossover junction endonuclease EME1, BRCA1, and CHAF1A.
TopBP1 interacts with BLM to maintain genome stability but is dispensable for preventing BLM degradation.
New
Niedzwiedz et al., Oxford, United Kingdom. In Mol Cell, Apr 2015
Finally, we identify critical residues that mediate interactions between TopBP1 and MDC1, and between BLM and TOP3A/RMI1/RMI2.
Top3-Rmi1 dissolve Rad51-mediated D loops by a topoisomerase-based mechanism.
New
Heyer et al., Davis, United States. In Mol Cell, Mar 2015
Also, the human Topoisomerase IIIa-RMI1-RMI2 complex is capable of dissolving D loops.
Structural Motifs Critical for In Vivo Function and Stability of the RecQ-Mediated Genome Instability Protein Rmi1.
Schmidt et al., Tampa, United States. In Plos One, 2014
Rmi1 is a member of the Sgs1/Top3/Rmi1 (STR) complex of Saccharomyces cerevisiae and has been implicated in binding and catalytic enhancement of Top3 in the dissolution of double Holliday junctions.
Accumulation and Phosphorylation of RecQ-Mediated Genome Instability Protein 1 (RMI1) at Serine 284 and Serine 292 during Mitosis.
Li et al., Tianjin, China. In Int J Mol Sci, 2014
BTR complex, composed of BLM, topoisomerase IIIα (Topo IIIα), RMI1 (RecQ-mediated genome instability protein 1, BLAP75) and RMI2 (RecQ-mediated genome instability protein 2, BLAP18), is crucial for maintaining genome stability.
DNA2 cooperates with the WRN and BLM RecQ helicases to mediate long-range DNA end resection in human cells.
Janscak et al., Zürich, Switzerland. In J Biol Chem, 2014
In addition, we present in vitro and in vivo data suggesting that BLM promotes DNA end resection as part of the BLM-TOPOIIIα-RMI1-RMI2 complex.
Holliday junction processing enzymes as guardians of genome stability.
Review
West et al., London, United Kingdom. In Trends Biochem Sci, 2014
In mammalian cells, HJs are processed by the BTR (BLM-topoisomerase IIIα-RMI1-RMI2) complex, the SLX-MUS (SLX1-SLX4-MUS81-EME1) complex, and the GEN1 resolvase.
Roles of SLX1-SLX4, MUS81-EME1, and GEN1 in avoiding genome instability and mitotic catastrophe.
West et al., London, United Kingdom. In Genes Dev, 2014
Three pathways for HJ processing exist in human cells and involve the following enzymes/complexes: BLM-TopoIIIα-RMI1-RMI2 (BTR complex), SLX1-SLX4-MUS81-EME1 (SLX-MUS complex), and GEN1.
Molecular mechanism of double Holliday junction dissolution.
Review
Costa et al., London, United Kingdom. In Cell Biosci, 2013
Within the dissolvasome, the RecQ-like BLM helicase provides the translocase function for Holliday junction migration, while the topoisomerase III alpha-RMI1 subcomplex works as a proficient DNA decatenase, together resulting in double-Holliday-junction unlinking.
The RTR complex as caretaker of genome stability and its unique meiotic function in plants.
Review
Puchta et al., Karlsruhe, Germany. In Front Plant Sci, 2013
The RTR complex consisting of a RecQ helicase, a type IA topoisomerase and the structural protein RMI1 is involved in the processing of DNA recombination intermediates in all eukaryotes.
Multifaceted role of the Topo IIIα-RMI1-RMI2 complex and DNA2 in the BLM-dependent pathway of DNA break end resection.
Sung et al., New Haven, United States. In Nucleic Acids Res, 2013
BLM exists in a complex with Topo IIIα, RMI1 and RMI2.
RMI1 promotes DNA replication fork progression and recovery from replication fork stress.
GeneRIF
Brown et al., Toronto, Canada. In Mol Cell Biol, 2012
RMI1 is required to promote normal replication fork progression
Glucose regulates RMI1 expression through the E2F pathways in adipose cells.
GeneRIF
Aramori et al., Tsukuba, Japan. In Endocrine, 2011
Glucose regulates RMI1 expression through the E2F pathways in adipose cells.
Aberrant chromosome morphology in human cells defective for Holliday junction resolution.
Impact
West et al., London, United Kingdom. In Nature, 2011
In human cells, the BLM protein, inactivated in individuals with Bloom's syndrome, acts in combination with topoisomerase IIIα, RMI1 and RMI2 (BTR complex) to promote the dissolution of double Holliday junctions.
RMI1 attenuates tumor development and is essential for early embryonic survival.
GeneRIF
Li et al., Houston, United States. In Mol Carcinog, 2011
These results demonstrated a dual-role of RMI1 in embryonic development and tumor suppression.
Adipocyte hyperplasia and RMI1 in the treatment of obesity.
Review
Shimokawa et al., Ibaraki, Japan. In Febs J, 2011
In this minireview, we focus on recQ-mediated genome instability 1 (RMI1), a recently identified novel molecular target for obesity treatment.
Crystal structures of RMI1 and RMI2, two OB-fold regulatory subunits of the BLM complex.
GeneRIF
Lei et al., Ann Arbor, United States. In Structure, 2010
Crystal structures of RMI1 and RMI2, two OB-fold regulatory subunits of the BLM complex
DNA end resection by Dna2-Sgs1-RPA and its stimulation by Top3-Rmi1 and Mre11-Rad50-Xrs2.
Impact
GeneRIF
Kowalczykowski et al., Davis, United States. In Nature, 2010
Study established that Dna2, Sgs1 and RPA constitute a minimal protein complex capable of DNA resection in vitro; in addition it was found that both the Top3 and Rmi1 complex and the Mre11-Rad50-Xrs2 complex have important roles as stimulatory components.
Specific pathways prevent duplication-mediated genome rearrangements.
Impact
Kolodner et al., San Diego, United States. In Nature, 2009
Numerous genes and pathways, including SGS1, TOP3, RMI1, SRS2, RAD6, SLX1, SLX4, SLX5, MSH2, MSH6, RAD10 and the DNA replication stress checkpoint requiring MRC1 and TOF1, were highly specific for suppressing these GCRs compared to GCRs mediated by single-copy sequences.
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