Proteinnsl1 Homolog, Chromosome 1 Open Reading Frame 48, C1orf48, MIS14

Total Page：16

File Type：pdf, Size：1020Kb

Proteinnsl1 Homolog, Chromosome 1 Open Reading Frame 48, C1orf48, MIS14

DATA SHEET NSL1 Human Recombinant Item Number rAP-3986 Synonyms NSL1 MIS12 Kinetochore Complex Component, NSL1 MIND Kinetochore Complex Component Homolog (S. Cerevisiae), Kinetochore-Associated ProteinNSL1 Homolog, Chromosome 1 Open Reading Frame 48, C1orf48, MIS14. Description NSL1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-281) and having a molecular mass of 34.6kDa.NSL1 is fused to a 23 amino acid His- tag at N-terminus & purified by proprietary chromatographic techniques. Uniprot Accesion Number Q96IY1 Amino Acid Sequence MGSSHHHHHH SSGLVPRGSH MGSMAGSPEL VVLDPPWDKE LAAGTESQAL VSATPREDFR VRCTSKRAVT EMLQLCGRFV QKLGDALPEE IREPALRDAQ WTFESAVQEN ISINGQAWQE AS- DNCFMDSD IKVLEDQFDE IIVDIATKRK QYPRKILECV IKTIKAKQEI LKQYHPVVHP LDLKYDPDPA PHMENLKCRG ETVAKEISEA MKSLPALIEQ GEGFSQVLRM QPVIHLQRIH QEVFSSCHRK PDAKPEN- FIT QIETTPTETA SRKTSDMVLK RKQTKDCPQR KWYPLRPKKI NLDT Source Escherichia Coli. Physical Appearance Sterile Filtered clear solution. Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C and Stability for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles. Formulation and Purity The NSL1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol. Greater than 85% as determined by SDS-PAGE. Application Solubility Biological Activity Shipping Format and Condition Lyophilized powder at room temperature. Optimal dilutions should be determined by each laboratory for each application. The listed dilutions are for recommendation only and the final condi- tions should be optimized by the ender users! This product is sold for Research Use Only Angio-Proteomie | 11 Park Drive, Suite 12 Boston, MA 02215, USA | Tel: 001‐617‐549‐2665 | Fax: 001‐480‐247‐4337 | Email： [email protected] .

Copy Link

Recommended publications

Analysis of Gene Expression Data for Gene Ontology
ANALYSIS OF GENE EXPRESSION DATA FOR GENE ONTOLOGY BASED PROTEIN FUNCTION PREDICTION A Thesis Presented to The Graduate Faculty of The University of Akron In Partial Fulfillment of the Requirements for the Degree Master of Science Robert Daniel Macholan May 2011 ANALYSIS OF GENE EXPRESSION DATA FOR GENE ONTOLOGY BASED PROTEIN FUNCTION PREDICTION Robert Daniel Macholan Thesis Approved: Accepted: _______________________________ _______________________________ Advisor Department Chair Dr. Zhong-Hui Duan Dr. Chien-Chung Chan _______________________________ _______________________________ Committee Member Dean of the College Dr. Chien-Chung Chan Dr. Chand K. Midha _______________________________ _______________________________ Committee Member Dean of the Graduate School Dr. Yingcai Xiao Dr. George R. Newkome _______________________________ Date ii ABSTRACT A tremendous increase in genomic data has encouraged biologists to turn to bioinformatics in order to assist in its interpretation and processing. One of the present challenges that need to be overcome in order to understand this data more completely is the development of a reliable method to accurately predict the function of a protein from its genomic information. This study focuses on developing an effective algorithm for protein function prediction. The algorithm is based on proteins that have similar expression patterns. The similarity of the expression data is determined using a novel measure, the slope matrix. The slope matrix introduces a normalized method for the comparison of expression levels throughout a proteome. The algorithm is tested using real microarray gene expression data. Their functions are characterized using gene ontology annotations. The results of the case study indicate the protein function prediction algorithm developed is comparable to the prediction algorithms that are based on the annotations of homologous proteins.
[Show full text]
The MIS12 Complex Is a Protein Interaction Hub for Outer Kinetochore Assembly
JCB: Article The MIS12 complex is a protein interaction hub for outer kinetochore assembly Arsen Petrovic,1 Sebastiano Pasqualato,1 Prakash Dube,3 Veronica Krenn,1 Stefano Santaguida,1 Davide Cittaro,4 Silvia Monzani,1 Lucia Massimiliano,1 Jenny Keller,1 Aldo Tarricone,1 Alessio Maiolica,1 Holger Stark,3 and Andrea Musacchio1,2 1Department of Experimental Oncology, European Institute of Oncology (IEO) and 2Research Unit of the Italian Institute of Technology, Italian Foundation for Cancer Research Institute of Molecular Oncology–IEO Campus, I-20139 Milan, Italy 33D Electron Cryomicroscopy Group, Max Planck Institute for Biophysical Chemistry, and Göttingen Center for Microbiology, University of Göttingen, 37077 Göttingen, Germany 4Consortium for Genomic Technologies, I-20139 Milan, Italy inetochores are nucleoprotein assemblies responsi axis of 22 nm. Through biochemical analysis, cross- ble for the attachment of chromosomes to spindle linking–based methods, and negative-stain electron mi K microtubules during mitosis. The KMN network, croscopy, we investigated the reciprocal organization of a crucial constituent of the outer kinetochore, creates an the subunits of the MIS12 complex and their contacts with interface that connects microtubules to centromeric chro the rest of the KMN network. A highlight of our findings matin. The NDC80, MIS12, and KNL1 complexes form the is the identification of the NSL1 subunit as a scaffold core of the KMN network. We recently reported the struc supporting interactions of the MIS12 complex with the tural organization of the human NDC80 complex. In this NDC80 and KNL1 complexes. Our analysis has important study, we extend our analysis to the human MIS12 com implications for understanding kinetochore organization in plex and show that it has an elongated structure with a long different organisms.
[Show full text]
Identification of Conserved Genes Triggering Puberty in European Sea
Blázquez et al. BMC Genomics (2017) 18:441 DOI 10.1186/s12864-017-3823-2 RESEARCHARTICLE Open Access Identification of conserved genes triggering puberty in European sea bass males (Dicentrarchus labrax) by microarray expression profiling Mercedes Blázquez1,2* , Paula Medina1,2,3, Berta Crespo1,4, Ana Gómez1 and Silvia Zanuy1* Abstract Background: Spermatogenesisisacomplexprocesscharacterized by the activation and/or repression of a number of genes in a spatio-temporal manner. Pubertal development in males starts with the onset of the first spermatogenesis and implies the division of primary spermatogonia and their subsequent entry into meiosis. This study is aimed at the characterization of genes involved in the onset of puberty in European sea bass, and constitutes the first transcriptomic approach focused on meiosis in this species. Results: European sea bass testes collected at the onset of puberty (first successful reproduction) were grouped in stage I (resting stage), and stage II (proliferative stage). Transition from stage I to stage II was marked by an increase of 11ketotestosterone (11KT), the main fish androgen, whereas the transcriptomic study resulted in 315 genes differentially expressed between the two stages. The onset of puberty induced 1) an up-regulation of genes involved in cell proliferation, cell cycle and meiosis progression, 2) changes in genes related with reproduction and growth, and 3) a down-regulation of genes included in the retinoic acid (RA) signalling pathway. The analysis of GO-terms and biological pathways showed that cell cycle, cell division, cellular metabolic processes, and reproduction were affected, consistent with the early events that occur during the onset of puberty.
[Show full text]
Reconstructing Cell Cycle Pseudo Time-Series Via Single-Cell Transcriptome Data—Supplement
School of Natural Sciences and Mathematics Reconstructing Cell Cycle Pseudo Time-Series Via Single-Cell Transcriptome Data—Supplement UT Dallas Author(s): Michael Q. Zhang Rights: CC BY 4.0 (Attribution) ©2017 The Authors Citation: Liu, Zehua, Huazhe Lou, Kaikun Xie, Hao Wang, et al. 2017. "Reconstructing cell cycle pseudo time-series via single-cell transcriptome data." Nature Communications 8, doi:10.1038/s41467-017-00039-z This document is being made freely available by the Eugene McDermott Library of the University of Texas at Dallas with permission of the copyright owner. All rights are reserved under United States copyright law unless specified otherwise. File name: Supplementary Information Description: Supplementary figures, supplementary tables, supplementary notes, supplementary methods and supplementary references. CCNE1 CCNE1 CCNE1 CCNE1 36 40 32 34 32 35 30 32 28 30 30 28 28 26 24 25 Normalized Expression Normalized Expression Normalized Expression Normalized Expression 26 G1 S G2/M G1 S G2/M G1 S G2/M G1 S G2/M Cell Cycle Stage Cell Cycle Stage Cell Cycle Stage Cell Cycle Stage CCNE1 CCNE1 CCNE1 CCNE1 40 32 40 40 35 30 38 30 30 28 36 25 26 20 20 34 Normalized Expression Normalized Expression Normalized Expression 24 Normalized Expression G1 S G2/M G1 S G2/M G1 S G2/M G1 S G2/M Cell Cycle Stage Cell Cycle Stage Cell Cycle Stage Cell Cycle Stage Supplementary Figure 1 | High stochasticity of single-cell gene expression means, as demonstrated by relative expression levels of gene Ccne1 using the mESC-SMARTer data. For every panel, 20 sample cells were randomly selected for each of the three stages, followed by plotting the mean expression levels at each stage.
[Show full text]
Assigning Function to Yeast Proteins by Integration of Technologies
Molecular Cell, Vol. 12, 1353–1365, December, 2003, Copyright 2003 by Cell Press Assigning Function to Yeast Proteins by Integration of Technologies Tony R. Hazbun,1,2 Lars Malmstro¨ m,3 Scott Anderson,4 proaches (Ito et al., 2001; Uetz et al., 2000); and many Beth J. Graczyk,3 Bethany Fox,3 Michael Riffle,3 of the proteins have been localized by indirect immuno- Bryan A. Sundin,3 J. Derringer Aranda,2 fluorescence or by fusion to green fluorescent protein W. Hayes McDonald,4 Chun-Hwei Chiu,3 (GFP) (Huh et al., 2003; Kumar et al., 2002; Ross-Mac- Brian E. Snydsman,3 Phillip Bradley,3 donald et al., 1999). Despite these large-scale studies, Eric G.D. Muller,3 Stanley Fields,1,2 David Baker,1,3 as well as numerous small-scale analyses, approxi- John R. Yates III,4 and Trisha N. Davis3,* mately one-third of the ORFs have not been assigned to 1Howard Hughes Medical Institute a functional category, indicating that large-scale studies 2 Departments of Genome Sciences and Medicine yield incomplete data sets and small-scale, focused 3 Department of Biochemistry studies tend to be biased toward specific areas of biol- University of Washington ogy. We focus here on an important subset of these Seattle, Washington 98195 uncharacterized ORFs, those that are essential for 4 Department of Cell Biology yeast viability. Scripps Research Institute Complete analysis of the yeast proteome requires La Jolla, California 92037 characterization of proteins refractory to analysis in pre- vious studies. We started with 100 ORFs that were known to be essential for viability but carried out un- Summary known functions.
[Show full text]
Massively Parallel Disruption of Enhancers Active During Human Corticogenesis
bioRxiv preprint doi: https://doi.org/10.1101/852673; this version posted December 2, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. Title: Massively parallel disruption of enhancers active during human corticogenesis Authors: Evan Geller1, Jake Gockley1§, Deena Emera1‡, Severin Uebbing1, Justin Cotney1+, James P. Noonan1,2,3* Affiliations: 1. Department of Genetics, Yale School of Medicine, New Haven, CT, 06510, USA. 2. Department of Neuroscience, Yale School of Medicine, New Haven, CT 06510, USA. 3. Kavli Institute for Neuroscience, Yale School of Medicine, New Haven, CT 06510, USA §Present address: Sage Bionetworks, Seattle, WA 98121, USA. +Present address: Department of Genetics and Genome Science, University of Connecticut Health, Farmington, CT 06030, USA ‡Present address: Center for Female Reproductive Longevity and Equality, Buck Institute for Research on Aging, Novato, CA 94945, USA *Corresponding author: [email protected]. bioRxiv preprint doi: https://doi.org/10.1101/852673; this version posted December 2, 2019. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC 4.0 International license. Abstract: Changes in gene regulation have been linked to the expansion of the human cerebral cortex and to neurodevelopmental disorders. However, the biological effects of genetic variation within developmental regulatory elements on human corticogenesis are not well understood.
[Show full text]
A High-Throughput Approach to Uncover Novel Roles of APOBEC2, a Functional Orphan of the AID/APOBEC Family
Rockefeller University Digital Commons @ RU Student Theses and Dissertations 2018 A High-Throughput Approach to Uncover Novel Roles of APOBEC2, a Functional Orphan of the AID/APOBEC Family Linda Molla Follow this and additional works at: https://digitalcommons.rockefeller.edu/ student_theses_and_dissertations Part of the Life Sciences Commons A HIGH-THROUGHPUT APPROACH TO UNCOVER NOVEL ROLES OF APOBEC2, A FUNCTIONAL ORPHAN OF THE AID/APOBEC FAMILY A Thesis Presented to the Faculty of The Rockefeller University in Partial Fulfillment of the Requirements for the degree of Doctor of Philosophy by Linda Molla June 2018 © Copyright by Linda Molla 2018 A HIGH-THROUGHPUT APPROACH TO UNCOVER NOVEL ROLES OF APOBEC2, A FUNCTIONAL ORPHAN OF THE AID/APOBEC FAMILY Linda Molla, Ph.D. The Rockefeller University 2018 APOBEC2 is a member of the AID/APOBEC cytidine deaminase family of proteins. Unlike most of AID/APOBEC, however, APOBEC2’s function remains elusive. Previous research has implicated APOBEC2 in diverse organisms and cellular processes such as muscle biology (in Mus musculus), regeneration (in Danio rerio), and development (in Xenopus laevis). APOBEC2 has also been implicated in cancer. However the enzymatic activity, substrate or physiological target(s) of APOBEC2 are unknown. For this thesis, I have combined Next Generation Sequencing (NGS) techniques with state-of-the-art molecular biology to determine the physiological targets of APOBEC2. Using a cell culture muscle differentiation system, and RNA sequencing (RNA-Seq) by polyA capture, I demonstrated that unlike the AID/APOBEC family member APOBEC1, APOBEC2 is not an RNA editor. Using the same system combined with enhanced Reduced Representation Bisulfite Sequencing (eRRBS) analyses I showed that, unlike the AID/APOBEC family member AID, APOBEC2 does not act as a 5-methyl-C deaminase.
[Show full text]
NSL1 (NM 001042549) Human Untagged Clone Product Data
OriGene Technologies, Inc. 9620 Medical Center Drive, Ste 200 Rockville, MD 20850, US Phone: +1-888-267-4436 [email protected] EU: [email protected] CN: [email protected] Product datasheet for SC311349 NSL1 (NM_001042549) Human Untagged Clone Product data: Product Type: Expression Plasmids Product Name: NSL1 (NM_001042549) Human Untagged Clone Tag: Tag Free Symbol: NSL1 Synonyms: C1orf48; DC8; MIS14 Vector: pCMV6-Entry (PS100001) E. coli Selection: Kanamycin (25 ug/mL) Cell Selection: Neomycin Fully Sequenced ORF: >NCBI ORF sequence for NM_001042549, the custom clone sequence may differ by one or more nucleotides ATGGCGGGGTCTCCTGAGTTGGTGGTCCTTGACCCTCCATGGGACAAGGAGCTCGCGGCTGGCACAGAGA GCCAGGCCTTGGTCTCCGCCACTCCCCGAGAAGACTTTCGGGTGCGCTGCACCTCGAAGCGGGCTGTGAC CGAAATGCTACAACTGTGCGGCCGCTTCGTGCAAAAGCTCGGGGACGCTCTGCCGGAGGAGATTCGGGAG CCCGCTCTGCGAGATGCGCAGTGGACTTTTGAATCAGCTGTGCAAGAGAATATCAGCATTAATGGGCAAG CATGGCAGGAAGCTTCAGATAATTGTTTTATGGATTCTGACATCAAAGTACTTGAAGATCAGTTTGATGA AATCATAGTAGATATAGCCACAAAACGTAAGCAGTATCCCAGAAAGATCCTGGAATGTGTCATCAAAACC ATAAAAGCAAAACAAGAAATTCTGAAGCAGTACCACCCTGTTGTACATCCACTGGACCTAAAATATGACC CTGATCCAGTTCTCAACGGGAATGCTTTCAACTTTTCCCCATTCAACATGATGTTGGCTGTGGATTTGTC ATATATGGTTTTTATTACTTCGAGCCCCTCATATGGAAAATTTGAAATGCAGAGGGGAAACAGTAGCAAA GGAGATCAGTGA Restriction Sites: SgfI-MluI ACCN: NM_001042549 OTI Disclaimer: Our molecular clone sequence data has been matched to the reference identifier above as a point of reference. Note that the complete sequence of our molecular clones may differ from the sequence published for this
[Show full text]
Phenotypic and Genotypic Characterization of Families With
www.nature.com/scientificreports OPEN Phenotypic and genotypic characterization of families with complex intellectual disability identifed pathogenic genetic variations in known and novel disease genes Hossein Darvish1,2, Luis J. Azcona3,4, Abbas Tafakhori5, Roxana Mesias3,6, Azadeh Ahmadifard7, Elena Sanchez3, Arman Habibi5, Elham Alehabib7, Amir Hossein Johari7, Babak Emamalizadeh8, Faezeh Jamali7, Marjan Chapi7, Javad Jamshidi9,10, Yuji Kajiwara11,12 & Coro Paisán-Ruiz4,12,13,14,15* Intellectual disability (ID), which presents itself during childhood, belongs to a group of neurodevelopmental disorders (NDDs) that are clinically widely heterogeneous and highly heritable, often being caused by single gene defects. Indeed, NDDs can be attributed to mutations at over 1000 loci, and all type of mutations, ranging from single nucleotide variations (SNVs) to large, complex copy number variations (CNVs), have been reported in patients with ID and other related NDDs. In this study, we recruited seven diferent recessive NDD families with comorbidities to perform a detailed clinical characterization and a complete genomic analysis that consisted of a combination of high throughput SNP-based genotyping and whole-genome sequencing (WGS). Diferent disease-associated loci and pathogenic gene mutations were identifed in each family, including known (n = 4) and novel (n = 2) mutations in known genes (NAGLU, SLC5A2, POLR3B, VPS13A, SYN1, SPG11), and the identifcation of a novel disease gene (n = 1; NSL1). Functional analyses were additionally performed in a gene associated with autism-like symptoms and epileptic seizures for further proof of pathogenicity. Lastly, detailed genotype-phenotype correlations were carried out to assist with the diagnosis of prospective families and to determine genomic variation with clinical relevance.
[Show full text]
Regulation of Outer Kinetochore Ndc80 Complex-Based Microtubule
Regulation of outer kinetochore Ndc80 complex-based PNAS PLUS microtubule attachments by the central kinetochore Mis12/MIND complex Emily M. Kudalkara,1, Emily A. Scarborougha, Neil T. Umbreita,2, Alex Zeltera, Daniel R. Gestauta,3, Michael Rifflea, Richard S. Johnsonb, Michael J. MacCossb, Charles L. Asburyc, and Trisha N. Davisa,4 aDepartment of Biochemistry, University of Washington, Seattle, WA 98195; bDepartment of Genome Sciences, University of Washington, Seattle, WA 98195; and cDepartment of Physiology and Biophysics, University of Washington, Seattle, WA 98195 Edited by Edward D. Korn, National Heart, Lung and Blood Institute, Bethesda, MD, and approved August 26, 2015 (received for review July 15, 2015) Multiple protein subcomplexes of the kinetochore cooperate as a Spc105, Mis12/MIND (Mtw1, Nsl1, Nnf1, Dsn1) complex, and cohesive molecular unit that forms load-bearing microtubule attach- Ndc80 (Ndc80, Nuf2, Spc24, Spc25) complex (5). In C. elegans, ments that drive mitotic chromosome movements. There is intriguing the 4-protein Ndc80 complex and Knl1 bind directly to micro- evidence suggesting that central kinetochore components influence tubules, but MIND does not. Instead, MIND serves as a struc- kinetochore–microtubule attachment, but the mechanism remains tural linker that connects DNA-binding components with the unclear. Here, we find that the conserved Mis12/MIND (Mtw1, microtubule-binding complexes (6, 7). The KMN complex binds Nsl1, Nnf1, Dsn1) and Ndc80 (Ndc80, Nuf2, Spc24, Spc25) com- microtubules with a higher affinity than Ndc80 complex or Knl1 plexes are connected by an extensive network of contacts, each alone, demonstrating that MIND can facilitate the synergistic essential for viability in cells, and collectively able to withstand sub- binding of outer kinetochore complexes.
[Show full text]
Spatiotemporal Dynamics of Spc105 Regulates the Assembly of the Drosophila Kinetochore Rsob.Royalsocietypublishing.Org Zsolt Venkei1,4, Marcin R
Spatiotemporal dynamics of Spc105 regulates the assembly of the Drosophila kinetochore rsob.royalsocietypublishing.org Zsolt Venkei1,4, Marcin R. Przewloka1, Yaseen Ladak1,3, Shahad Albadri1,†, Alex Sossick2, Gabor Juhasz4,Be´la Nova´k3 Research and David M. Glover1 Cite this article: Venkei Z, Przewloka MR, 1Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK Ladak Y, Albadri S, Sossick A, Juhasz G, Nova´k 2Wellcome Trust/Cancer Research UK Gurdon Institute, Cambridge CB2 1QN, UK B, Glover DM. 2012 Spatiotemporal dynamics 3Oxford Centre for Integrative Systems Biology, Department of Biochemistry, University of Spc105 regulates the assembly of the of Oxford, Oxford OX1 3QU, UK Drosophila kinetochore. Open Biol 2: 110032. 4Department of Anatomy, Cell and Developmental Biology, Eotvos Lorand University, http://dx.doi.org/10.1098/rsob.110032 Budapest 1117, Hungary Received: 24 November 2011 1. Summary Accepted: 17 January 2012 The formation of kinetochores shortly before each cell division is a prerequisite for proper chromosome segregation. The synchronous mitoses of Drosophila syncytial embryos have provided an ideal in vivo system to follow kinetochore assembly kinetics and so address the question of how kinetochore formation is regulated. We found that the nuclear exclusion of the Spc105/KNL1 protein Subject Area: during interphase prevents precocious assembly of the Mis12 complex. The cellular biology/molecular biology/genetics nuclear import of Spc105 in early prophase and its immediate association with the Mis12 complex on centromeres are thus the first steps in kinetochore Keywords: assembly. The cumulative kinetochore levels of Spc105 and Mis12 complex centromere, chromosomes, KMN network, then determine the rate of Ndc80 complex recruitment commencing only Mis12 complex, mitosis after nuclear envelope breakdown.
[Show full text]
Bridgin Connects the Outer Kinetochore to Centromeric Chromatin ✉ ✉ Shreyas Sridhar 1,4, Tetsuya Hori2, Reiko Nakagawa 3, Tatsuo Fukagawa 2 & Kaustuv Sanyal 1,2
ARTICLE https://doi.org/10.1038/s41467-020-20161-9 OPEN Bridgin connects the outer kinetochore to centromeric chromatin ✉ ✉ Shreyas Sridhar 1,4, Tetsuya Hori2, Reiko Nakagawa 3, Tatsuo Fukagawa 2 & Kaustuv Sanyal 1,2 The microtubule-binding outer kinetochore is coupled to centromeric chromatin through CENP-CMif2, CENP-TCnn1, and CENP-UAme1 linker pathways originating from the constitutive centromere associated network (CCAN) of the inner kinetochore. Here, we demonstrate the 1234567890():,; recurrent loss of most CCAN components, including certain kinetochore linkers during the evolution of the fungal phylum of Basidiomycota. By kinetochore interactome analyses in a model basidiomycete and human pathogen Cryptococcus neoformans, a forkhead-associated domain containing protein “bridgin” was identiﬁed as a kinetochore component along with other predicted kinetochore proteins. In vivo and in vitro functional analyses of bridgin reveal its ability to connect the outer kinetochore with centromeric chromatin to ensure accurate chromosome segregation. Unlike established CCAN-based linkers, bridgin is recruited at the outer kinetochore establishing its role as a distinct family of kinetochore proteins. Presence of bridgin homologs in non-fungal lineages suggests an ancient divergent strategy exists to bridge the outer kinetochore with centromeric chromatin. 1 Molecular Mycology Laboratory, Molecular Biology and Genetics Unit, Jawaharlal Nehru Center for Advanced Scientiﬁc Research (JNCASR), Bangalore, India 560064. 2 Laboratory of Chromosome
[Show full text]