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  • 2005-2009  (233)
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  • 1
    Publication Date: 2008-06-06
    Description: High-harmonic generation by focusing a femtosecond laser onto a gas is a well-known method of producing coherent extreme-ultraviolet (EUV) light. This nonlinear conversion process requires high pulse intensities, greater than 10(13) W cm(-2), which are not directly attainable using only the output power of a femtosecond oscillator. Chirped-pulse amplification enables the pulse intensity to exceed this threshold by incorporating several regenerative and/or multi-pass amplifier cavities in tandem. Intracavity pulse amplification (designed not to reduce the pulse repetition rate) also requires a long cavity. Here we demonstrate a method of high-harmonic generation that requires no extra cavities. This is achieved by exploiting the local field enhancement induced by resonant plasmons within a metallic nanostructure consisting of bow-tie-shaped gold elements on a sapphire substrate. In our experiment, the output beam emitted from a modest femtosecond oscillator (100-kW peak power, 1.3-nJ pulse energy and 10-fs pulse duration) is directly focused onto the nanostructure with a pulse intensity of only 10(11) W cm(-2). The enhancement factor exceeds 20 dB, which is sufficient to produce EUV wavelengths down to 47 nm by injection with an argon gas jet. The method could form the basis for constructing laptop-sized EUV light sources for advanced lithography and high-resolution imaging applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Seungchul -- Jin, Jonghan -- Kim, Young-Jin -- Park, In-Yong -- Kim, Yunseok -- Kim, Seung-Woo -- England -- Nature. 2008 Jun 5;453(7196):757-60. doi: 10.1038/nature07012.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Billionth Uncertainty Precision Engineering Group, KAIST, Daedeok Science Town, Daejeon 305-701, South Korea.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18528390" target="_blank"〉PubMed〈/a〉
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    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 2
    Publication Date: 2009-07-10
    Description: Recent advances in sequencing technologies have initiated an era of personal genome sequences. To date, human genome sequences have been reported for individuals with ancestry in three distinct geographical regions: a Yoruba African, two individuals of northwest European origin, and a person from China. Here we provide a highly annotated, whole-genome sequence for a Korean individual, known as AK1. The genome of AK1 was determined by an exacting, combined approach that included whole-genome shotgun sequencing (27.8x coverage), targeted bacterial artificial chromosome sequencing, and high-resolution comparative genomic hybridization using custom microarrays featuring more than 24 million probes. Alignment to the NCBI reference, a composite of several ethnic clades, disclosed nearly 3.45 million single nucleotide polymorphisms (SNPs), including 10,162 non-synonymous SNPs, and 170,202 deletion or insertion polymorphisms (indels). SNP and indel densities were strongly correlated genome-wide. Applying very conservative criteria yielded highly reliable copy number variants for clinical considerations. Potential medical phenotypes were annotated for non-synonymous SNPs, coding domain indels, and structural variants. The integration of several human whole-genome sequences derived from several ethnic groups will assist in understanding genetic ancestry, migration patterns and population bottlenecks.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2860965/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2860965/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, Jong-Il -- Ju, Young Seok -- Park, Hansoo -- Kim, Sheehyun -- Lee, Seonwook -- Yi, Jae-Hyuk -- Mudge, Joann -- Miller, Neil A -- Hong, Dongwan -- Bell, Callum J -- Kim, Hye-Sun -- Chung, In-Soon -- Lee, Woo-Chung -- Lee, Ji-Sun -- Seo, Seung-Hyun -- Yun, Ji-Young -- Woo, Hyun Nyun -- Lee, Heewook -- Suh, Dongwhan -- Lee, Seungbok -- Kim, Hyun-Jin -- Yavartanoo, Maryam -- Kwak, Minhye -- Zheng, Ying -- Lee, Mi Kyeong -- Park, Hyunjun -- Kim, Jeong Yeon -- Gokcumen, Omer -- Mills, Ryan E -- Zaranek, Alexander Wait -- Thakuria, Joseph -- Wu, Xiaodi -- Kim, Ryan W -- Huntley, Jim J -- Luo, Shujun -- Schroth, Gary P -- Wu, Thomas D -- Kim, HyeRan -- Yang, Kap-Seok -- Park, Woong-Yang -- Kim, Hyungtae -- Church, George M -- Lee, Charles -- Kingsmore, Stephen F -- Seo, Jeong-Sun -- HG004221/HG/NHGRI NIH HHS/ -- P20 RR016480/RR/NCRR NIH HHS/ -- P20 RR016480-08/RR/NCRR NIH HHS/ -- RR016480/RR/NCRR NIH HHS/ -- U01 AI066569/AI/NIAID NIH HHS/ -- U01 AI066569-04/AI/NIAID NIH HHS/ -- U19 HD077693/HD/NICHD NIH HHS/ -- England -- Nature. 2009 Aug 20;460(7258):1011-5. doi: 10.1038/nature08211. Epub 2009 Jul 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genomic Medicine Institute, Medical Research Center, Seoul National University, Seoul 110-799, Korea.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19587683" target="_blank"〉PubMed〈/a〉
    Keywords: Asian Continental Ancestry Group/*genetics ; Chromosomes, Artificial, Bacterial/genetics ; Comparative Genomic Hybridization ; Computational Biology ; Genome, Human/*genetics ; Humans ; INDEL Mutation/genetics ; Korea ; Oligonucleotide Array Sequence Analysis ; Polymorphism, Single Nucleotide/genetics ; Sequence Analysis, DNA
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  • 3
    Publication Date: 2009-05-05
    Description: Substrates of the proteasome are recognized and unfolded by the regulatory particle, and then translocated into the core particle (CP) to be degraded. A hetero-hexameric ATPase ring, containing subunits Rpt1-6, is situated within the base subassembly of the regulatory particle. The ATPase ring sits atop the CP, with the Rpt carboxy termini inserted into pockets in the CP. Here we identify a previously unknown function of the Rpt proteins in proteasome biogenesis through deleting the C-terminal residue from each Rpt in the yeast Saccharomyces cerevisiae. Our results indicate that assembly of the hexameric ATPase ring is templated on the CP. We have also identified an apparent intermediate in base assembly, BP1, which contains Rpn1, three Rpts and Hsm3, a chaperone for base assembly. The Rpt proteins with the strongest assembly phenotypes, Rpt4 and Rpt6, were absent from BP1. We propose that Rpt4 and Rpt6 form a nucleating complex to initiate base assembly, and that this complex is subsequently joined by BP1 to complete the Rpt ring. Our studies show that assembly of the proteasome base is a rapid yet highly orchestrated process.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2722381/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2722381/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, Soyeon -- Roelofs, Jeroen -- Kim, Woong -- Robert, Jessica -- Schmidt, Marion -- Gygi, Steven P -- Finley, Daniel -- 5F32GM75737-2/GM/NIGMS NIH HHS/ -- F32 GM075737-01A2/GM/NIGMS NIH HHS/ -- GM043601/GM/NIGMS NIH HHS/ -- GM67945/GM/NIGMS NIH HHS/ -- R01 GM084228/GM/NIGMS NIH HHS/ -- England -- Nature. 2009 Jun 11;459(7248):866-70. doi: 10.1038/nature08065.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19412160" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases/*chemistry/genetics/*metabolism ; Molecular Chaperones/metabolism ; Proteasome Endopeptidase Complex/*biosynthesis/*chemistry/genetics/metabolism ; Saccharomyces cerevisiae/*enzymology/genetics ; Saccharomyces cerevisiae Proteins/chemistry/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 4
    Publication Date: 2006-04-08
    Description: The selection and assembly of materials are central issues in the development of smaller, more flexible batteries. Cobalt oxide has shown excellent electrochemical cycling properties and is thus under consideration as an electrode for advanced lithium batteries. We used viruses to synthesize and assemble nanowires of cobalt oxide at room temperature. By incorporating gold-binding peptides into the filament coat, we formed hybrid gold-cobalt oxide wires that improved battery capacity. Combining virus-templated synthesis at the peptide level and methods for controlling two-dimensional assembly of viruses on polyelectrolyte multilayers provides a systematic platform for integrating these nanomaterials to form thin, flexible lithium ion batteries.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nam, Ki Tae -- Kim, Dong-Wan -- Yoo, Pil J -- Chiang, Chung-Yi -- Meethong, Nonglak -- Hammond, Paula T -- Chiang, Yet-Ming -- Belcher, Angela M -- New York, N.Y. -- Science. 2006 May 12;312(5775):885-8. Epub 2006 Apr 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Materials Science and Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601154" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacteriophage M13/chemistry/genetics ; Capsid Proteins/chemistry ; *Cobalt/chemistry ; Crystallization ; Electric Conductivity ; *Electric Power Supplies ; Electrochemistry ; *Electrodes ; Gold ; Lithium ; Microscopy, Electron, Transmission ; *Nanostructures ; *Nanotechnology ; *Oxides/chemistry ; Peptide Library ; Protein Engineering ; Temperature ; Thermodynamics
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
    Publication Date: 2007-05-19
    Description: Mauna Loa volcano, Hawaii, deforms by a combination of shallow dike intrusions in the rift zones and earthquakes along the base of the volcano, but it is not known how the spreading is accommodated in the lower part of the volcanic edifice. We present evidence from interferometric synthetic aperture radar data for secular inflation of a dike-like magma body at intermediate depth in the southwest rift zone during 2002 to 2005. Magma accumulation occurred in a section of the rift zone that was unclamped by previous dikes and earthquakes, suggesting that stress transfer plays an important role in controlling subsurface magma accumulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amelung, Falk -- Yun, Sang-Ho -- Walter, Thomas R -- Segall, Paul -- Kim, Sang-Wan -- New York, N.Y. -- Science. 2007 May 18;316(5827):1026-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosenstiel School of Marine and Atmospheric Sciences, University of Miami, 4600 Rickenbacker Causeway, Miami, FL 33149, USA. famelung@rsmas.miami.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17510364" target="_blank"〉PubMed〈/a〉
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  • 6
    Publication Date: 2006-12-23
    Description: Synonymous single-nucleotide polymorphisms (SNPs) do not produce altered coding sequences, and therefore they are not expected to change the function of the protein in which they occur. We report that a synonymous SNP in the Multidrug Resistance 1 (MDR1) gene, part of a haplotype previously linked to altered function of the MDR1 gene product P-glycoprotein (P-gp), nonetheless results in P-gp with altered drug and inhibitor interactions. Similar mRNA and protein levels, but altered conformations, were found for wild-type and polymorphic P-gp. We hypothesize that the presence of a rare codon, marked by the synonymous polymorphism, affects the timing of cotranslational folding and insertion of P-gp into the membrane, thereby altering the structure of substrate and inhibitor interaction sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kimchi-Sarfaty, Chava -- Oh, Jung Mi -- Kim, In-Wha -- Sauna, Zuben E -- Calcagno, Anna Maria -- Ambudkar, Suresh V -- Gottesman, Michael M -- Intramural NIH HHS/ -- New York, N.Y. -- Science. 2007 Jan 26;315(5811):525-8. Epub 2006 Dec 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA. kimchi@cber.fda.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17185560" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cell Membrane/metabolism ; Cercopithecus aethiops ; Codon ; Cyclosporine/pharmacology ; *Genes, MDR ; Haplotypes ; HeLa Cells ; Humans ; Mutagenesis, Site-Directed ; P-Glycoprotein/antagonists & inhibitors/*chemistry/genetics/*metabolism ; *Polymorphism, Single Nucleotide ; Protein Biosynthesis ; Protein Conformation ; *Protein Folding ; Protein Structure, Tertiary ; RNA, Messenger/genetics/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Rhodamine 123/metabolism/pharmacology ; Sirolimus/pharmacology ; Substrate Specificity ; Transfection ; Verapamil/metabolism/pharmacology
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  • 7
    Publication Date: 2009-12-08
    Description: We report an improved draft nucleotide sequence of the 2.3-gigabase genome of maize, an important crop plant and model for biological research. Over 32,000 genes were predicted, of which 99.8% were placed on reference chromosomes. Nearly 85% of the genome is composed of hundreds of families of transposable elements, dispersed nonuniformly across the genome. These were responsible for the capture and amplification of numerous gene fragments and affect the composition, sizes, and positions of centromeres. We also report on the correlation of methylation-poor regions with Mu transposon insertions and recombination, and copy number variants with insertions and/or deletions, as well as how uneven gene losses between duplicated regions were involved in returning an ancient allotetraploid to a genetically diploid state. These analyses inform and set the stage for further investigations to improve our understanding of the domestication and agricultural improvements of maize.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schnable, Patrick S -- Ware, Doreen -- Fulton, Robert S -- Stein, Joshua C -- Wei, Fusheng -- Pasternak, Shiran -- Liang, Chengzhi -- Zhang, Jianwei -- Fulton, Lucinda -- Graves, Tina A -- Minx, Patrick -- Reily, Amy Denise -- Courtney, Laura -- Kruchowski, Scott S -- Tomlinson, Chad -- Strong, Cindy -- Delehaunty, Kim -- Fronick, Catrina -- Courtney, Bill -- Rock, Susan M -- Belter, Eddie -- Du, Feiyu -- Kim, Kyung -- Abbott, Rachel M -- Cotton, Marc -- Levy, Andy -- Marchetto, Pamela -- Ochoa, Kerri -- Jackson, Stephanie M -- Gillam, Barbara -- Chen, Weizu -- Yan, Le -- Higginbotham, Jamey -- Cardenas, Marco -- Waligorski, Jason -- Applebaum, Elizabeth -- Phelps, Lindsey -- Falcone, Jason -- Kanchi, Krishna -- Thane, Thynn -- Scimone, Adam -- Thane, Nay -- Henke, Jessica -- Wang, Tom -- Ruppert, Jessica -- Shah, Neha -- Rotter, Kelsi -- Hodges, Jennifer -- Ingenthron, Elizabeth -- Cordes, Matt -- Kohlberg, Sara -- Sgro, Jennifer -- Delgado, Brandon -- Mead, Kelly -- Chinwalla, Asif -- Leonard, Shawn -- Crouse, Kevin -- Collura, Kristi -- Kudrna, Dave -- Currie, Jennifer -- He, Ruifeng -- Angelova, Angelina -- Rajasekar, Shanmugam -- Mueller, Teri -- Lomeli, Rene -- Scara, Gabriel -- Ko, Ara -- Delaney, Krista -- Wissotski, Marina -- Lopez, Georgina -- Campos, David -- Braidotti, Michele -- Ashley, Elizabeth -- Golser, Wolfgang -- Kim, HyeRan -- Lee, Seunghee -- Lin, Jinke -- Dujmic, Zeljko -- Kim, Woojin -- Talag, Jayson -- Zuccolo, Andrea -- Fan, Chuanzhu -- Sebastian, Aswathy -- Kramer, Melissa -- Spiegel, Lori -- Nascimento, Lidia -- Zutavern, Theresa -- Miller, Beth -- Ambroise, Claude -- Muller, Stephanie -- Spooner, Will -- Narechania, Apurva -- Ren, Liya -- Wei, Sharon -- Kumari, Sunita -- Faga, Ben -- Levy, Michael J -- McMahan, Linda -- Van Buren, Peter -- Vaughn, Matthew W -- Ying, Kai -- Yeh, Cheng-Ting -- Emrich, Scott J -- Jia, Yi -- Kalyanaraman, Ananth -- Hsia, An-Ping -- Barbazuk, W Brad -- Baucom, Regina S -- Brutnell, Thomas P -- Carpita, Nicholas C -- Chaparro, Cristian -- Chia, Jer-Ming -- Deragon, Jean-Marc -- Estill, James C -- Fu, Yan -- Jeddeloh, Jeffrey A -- Han, Yujun -- Lee, Hyeran -- Li, Pinghua -- Lisch, Damon R -- Liu, Sanzhen -- Liu, Zhijie -- Nagel, Dawn Holligan -- McCann, Maureen C -- SanMiguel, Phillip -- Myers, Alan M -- Nettleton, Dan -- Nguyen, John -- Penning, Bryan W -- Ponnala, Lalit -- Schneider, Kevin L -- Schwartz, David C -- Sharma, Anupma -- Soderlund, Carol -- Springer, Nathan M -- Sun, Qi -- Wang, Hao -- Waterman, Michael -- Westerman, Richard -- Wolfgruber, Thomas K -- Yang, Lixing -- Yu, Yeisoo -- Zhang, Lifang -- Zhou, Shiguo -- Zhu, Qihui -- Bennetzen, Jeffrey L -- Dawe, R Kelly -- Jiang, Jiming -- Jiang, Ning -- Presting, Gernot G -- Wessler, Susan R -- Aluru, Srinivas -- Martienssen, Robert A -- Clifton, Sandra W -- McCombie, W Richard -- Wing, Rod A -- Wilson, Richard K -- New York, N.Y. -- Science. 2009 Nov 20;326(5956):1112-5. doi: 10.1126/science.1178534.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Plant Genomics, Iowa State University, Ames, IA 50011, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965430" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Centromere/genetics ; Chromosome Mapping ; Chromosomes, Plant/genetics ; Crops, Agricultural/genetics ; DNA Copy Number Variations ; DNA Methylation ; DNA Transposable Elements ; DNA, Plant/genetics ; Genes, Plant ; *Genetic Variation ; *Genome, Plant ; Inbreeding ; MicroRNAs/genetics ; Molecular Sequence Data ; Ploidies ; RNA, Plant/genetics ; Recombination, Genetic ; Retroelements ; *Sequence Analysis, DNA ; Zea mays/*genetics
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  • 8
    Publication Date: 2008-07-26
    Description: Brassinosteroids (BRs) bind to the extracellular domain of the receptor kinase BRI1 to activate a signal transduction cascade that regulates nuclear gene expression and plant development. Many components of the BR signaling pathway have been identified and studied in detail. However, the substrate of BRI1 kinase that transduces the signal to downstream components remains unknown. Proteomic studies of plasma membrane proteins lead to the identification of three homologous BR-signaling kinases (BSK1, BSK2, and BSK3). The BSKs are phosphorylated by BRI1 in vitro and interact with BRI1 in vivo. Genetic and transgenic studies demonstrate that the BSKs represent a small family of kinases that activate BR signaling downstream of BRI1. These results demonstrate that BSKs are the substrates of BRI1 kinase that activate downstream BR signal transduction.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2730546/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2730546/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, Wenqiang -- Kim, Tae-Wuk -- Oses-Prieto, Juan A -- Sun, Yu -- Deng, Zhiping -- Zhu, Shengwei -- Wang, Ruiju -- Burlingame, Alma L -- Wang, Zhi-Yong -- R01 GM066258/GM/NIGMS NIH HHS/ -- R01 GM066258-07/GM/NIGMS NIH HHS/ -- R01GM066258/GM/NIGMS NIH HHS/ -- RR012961/RR/NCRR NIH HHS/ -- RR01614/RR/NCRR NIH HHS/ -- RR019934/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 2008 Jul 25;321(5888):557-60. doi: 10.1126/science.1156973.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18653891" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/enzymology/genetics/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Brassinosteroids ; Cell Membrane/metabolism ; Cholestanols/metabolism/pharmacology ; Molecular Sequence Data ; Mutagenesis, Insertional ; Phosphorylation ; Plants, Genetically Modified ; Protein Kinases/chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases ; Proteomics ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Steroids, Heterocyclic/metabolism/pharmacology
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  • 9
    Publication Date: 2008-07-26
    Description: Chromosome segregation, transcriptional regulation, and repair of DNA double-strand breaks require the cohesin protein complex. Cohesin holds the replicated chromosomes (sister chromatids) together to mediate sister chromatid cohesion. The mechanism of how cohesion is established is unknown. We found that in budding yeast, the head domain of the Smc3p subunit of cohesin is acetylated by the Eco1p acetyltransferase at two evolutionarily conserved residues, promoting the chromatin-bound cohesin to tether sister chromatids. Smc3p acetylation is induced in S phase after the chromatin loading of cohesin and is suppressed in G(1) and G(2)/M. Smc3 head acetylation and its cell cycle regulation provide important insights into the biology and mechanism of cohesion establishment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Unal, Elcin -- Heidinger-Pauli, Jill M -- Kim, Woong -- Guacci, Vincent -- Onn, Itay -- Gygi, Steven P -- Koshland, Douglas E -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Jul 25;321(5888):566-9. doi: 10.1126/science.1157880.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Embryology, Carnegie Institution, 3520 San Martin Drive, Baltimore, MD 21218, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18653894" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetyltransferases/genetics/*metabolism ; Amino Acid Sequence ; Amino Acid Substitution ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; Cell Division ; Chondroitin Sulfate Proteoglycans/chemistry/genetics/*metabolism ; Chromatids/*physiology ; Chromatin/metabolism ; Chromosomal Proteins, Non-Histone/chemistry/genetics/*metabolism ; Chromosomes, Fungal/*physiology ; G1 Phase ; G2 Phase ; Immunoprecipitation ; Lysine/metabolism ; Molecular Sequence Data ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Protein Structure, Tertiary ; S Phase ; Saccharomyces cerevisiae/genetics/growth & development/*physiology ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism
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  • 10
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