Thomas R. Beattie

McGill University

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Shu Shu Yang

Yunnan University

Stephen D. Bell

Indiana University Bloomington

Rodrigo Reyes‐Lamothe

McGill University

Nitin Kapadia

The Francis Crick Institute

ÉN

Émilien Nicolas

Université Libre de Bruxelles

Mark C. Leake

University of York

Stephan Uphoff

Science Oxford

Angela Yu

McGill University

Huan Zheng

Nanjing Agricultural University

Adam J. M. Wollman

University of York

Cooperative Institutions

Merck & Co., Inc., Rahway, NJ, USA (United States)

University of Oxford

McGill University

Institute of Structural and Molecular Biology

CIC bioGUNE

Harvard University

Indiana University Bloomington

Centro de Investigación Biomédica en Red de Enfermedades Hepáticas y Digestivas

Merck (Japan)

University of Edinburgh

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Senior Chemists Committee: Making progress

C&EN Global Enterprise (2017)

Thomas R. Beattie

The Senior Chemists Committee's mission is to address and support the needs and ambitions of senior chemists and to use their experience and knowledge. As the newest ACS national committee, we are keenly interested in measuring our progress as we proceed. We have made strides in the past year. For example, to facilitate better communication with our constituents, we have replaced our e-mail address with seniorchemists@acs.org. This easily recognizable e-mail address will be the point of contact for both outgoing messages, such as the Newsletter for Senior Chemists, and incoming feedback, such as responses on our Senior Chemists Group on the ACS Network, as well as general inquiries. This modification to the e-mail address has increased our newsletter open rate by 25%, a substantial increase considering that our e-mails are distributed to 45,000 recipients. We have also expanded our recognition efforts. ACS has long honored 50- and 60-year members. During

10.1021/cen-09522-comment

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Synthesis of dl-1-deoxy-1-fluoro-6-O-methyl-chiro-inositol: confirmation of a structural-DAST fluorination correlation

Carbohydrate Research (1993)

Shu Shu Yang Yuang-ching P. Chiang Thomas R. Beattie

10.1016/0008-6215(93)84074-g

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Citations (8)

Consulting for Seniors: Having It Your Way

ACS symposium series (2014)

Thomas R. Beattie

Consulting can provide professional satisfaction and some personal income for senior/retired chemists. The author reviews, based on his own consulting experiences, the many factors that lead to a successful consulting business using accumulated personal knowledge and experience. Consulting may not work for everyone. Although it is difficult to do full-time, there are many avenues to explore in looking for part-time consulting. If you try it, it can be invigorating and stimulating. If you try it and it is not working well for you, get rid of it quickly and find other things to enjoy.

Information technology consulting

10.1021/bk-2014-1169.ch012

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DAST (diethylaminosulfur trifluoride) induced epimerization of a 2-(acetoxymethyl)myoinositol

The Journal of Organic Chemistry (1981)

Shu Shu Yang Thomas R. Beattie

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTDAST (diethylaminosulfur trifluoride) induced epimerization of a 2-(acetoxymethyl)myoinositolShu Shu Yang and Thomas R. BeattieCite this: J. Org. Chem. 1981, 46, 8, 1718–1720Publication Date (Print):April 1, 1981Publication History Published online1 May 2002Published inissue 1 April 1981https://pubs.acs.org/doi/10.1021/jo00321a038https://doi.org/10.1021/jo00321a038research-articleACS PublicationsRequest reuse permissionsArticle Views256Altmetric-Citations19LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts

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10.1021/jo00321a038

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Citations (19)

Identification and characterization of a heterotrimeric archaeal DNA polymerase holoenzyme

Nature Communications (2017)

Jiangyu Yan Thomas R. Beattie Adriana L. Rojas Kelly M. Schermerhorn Tamzin Gristwood

Abstract Since their initial characterization over 30 years ago, it has been believed that the archaeal B-family DNA polymerases are single-subunit enzymes. This contrasts with the multi-subunit B-family replicative polymerases of eukaryotes. Here we reveal that the highly studied PolB1 from Sulfolobus solfataricus exists as a heterotrimeric complex in cell extracts. Two small subunits, PBP1 and PBP2, associate with distinct surfaces of the larger catalytic subunit and influence the enzymatic properties of the DNA polymerase. Thus, multi-subunit replicative DNA polymerase holoenzymes are present in all three domains of life. We reveal the architecture of the assembly by a combination of cross-linking coupled with mass spectrometry, X-ray crystallography and single-particle electron microscopy. The small subunits stabilize the holoenzyme assembly and the acidic tail of one small subunit mitigates the ability of the enzyme to perform strand-displacement synthesis, with important implications for lagging strand DNA synthesis.

Sulfolobus solfataricus

DNA clamp

Specificity factor

Replisome

Crenarchaeota

DNA polymerase II

Primase

10.1038/ncomms15075

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The molecular biology of DNA replication in the archaeon Sulfolobus solfataricus

Thomas R. Beattie

DNA replication is essential for the propagation of all living organisms. The ability of a cell to accurately duplicate its entire genome is dependent upon the activity of numerous proteins. Identifying the molecular mechanisms by which these proteins act, and determining how they are physically and functionally coordinated at sites of active DNA replication, is central to understanding this essential cellular process. Archaea possess a DNA replication machinery which is ancestral to the one present in eukaryotes, and thus these organisms serve as simplified model systems for understanding the complexities of eukaryotic DNA replication. This thesis investigates the molecular mechanisms underlying Okazaki fragment maturation in the crenarchaeon Sulfolobus solfataricus, which is essential to the completion of lagging strand DNA replication. Reconstitution of Okazaki fragment maturation in vitro demonstrated that the activities of three enzymes – PolB1, Fen1, and Lig1 – are required for this process in S. solfataricus. Furthermore, it was shown that optimum coordination of their three distinct activities is dependent on the ability of PolB1, Fen1 and Lig1 to simultaneously interact with a single PCNA ring, providing evidence for a mechanism of multi-enzyme coordination which may be universally employed by DNA sliding clamp proteins. The importance of protein flexibility in the accommodation of multiple proteins around a single PCNA was also investigated. Finally, the physical coordination of one of these key maturation enzymes – PolB1 – with other replisome proteins was examined. It was demonstrated that PolB1 exists in a trimeric complex in vivo with two previously unidentified factors, raising the possibility of uncharacterised activities and interactions for this crucial enzyme. Taken together, these data provide new insights into functionally important protein-protein interactions within the archaeal replisome, and facilitate a greater understanding of the DNA replication machinery in both archaea and eukaryotes.

Okazaki fragments

Sulfolobus solfataricus

Replisome

Pre-replication complex

Replication factor C

DNA clamp

Origin recognition complex

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Frequent exchange of the DNA polymerase during bacterial chromosome replication

eLife (2017)

Thomas R. Beattie Nitin Kapadia Émilien Nicolas Stephan Uphoff Adam J. M. Wollman

The replisome is a multiprotein machine that carries out DNA replication. In Escherichia coli, a single pair of replisomes is responsible for duplicating the entire 4.6 Mbp circular chromosome. In vitro studies of reconstituted E. coli replisomes have attributed this remarkable processivity to the high stability of the replisome once assembled on DNA. By examining replisomes in live E. coli with fluorescence microscopy, we found that the Pol III* subassembly frequently disengages from the replisome during DNA synthesis and exchanges with free copies from solution. In contrast, the DnaB helicase associates stably with the replication fork, providing the molecular basis for how the E. coli replisome can maintain high processivity and yet possess the flexibility to bypass obstructions in template DNA. Our data challenges the widely-accepted semi-discontinuous model of chromosomal replication, instead supporting a fully discontinuous mechanism in which synthesis of both leading and lagging strands is frequently interrupted.

Replisome

Processivity

dnaB helicase

Pre-replication complex

DNA clamp

10.7554/elife.21763

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Citations (123)

The role of the DNA sliding clamp in Okazaki fragment maturation in archaea and eukaryotes

Biochemical Society Transactions (2011)

Thomas R. Beattie Stephen D. Bell

Efficient processing of Okazaki fragments generated during discontinuous lagging-strand DNA replication is critical for the maintenance of genome integrity. In eukaryotes, a number of enzymes co-ordinate to ensure the removal of initiating primers from the 5′-end of each fragment and the generation of a covalently linked daughter strand. Studies in eukaryotic systems have revealed that the co-ordination of DNA polymerase δ and FEN-1 (Flap Endonuclease 1) is sufficient to remove the majority of primers. Other pathways such as that involving Dna2 also operate under certain conditions, although, notably, Dna2 is not universally conserved between eukaryotes and archaea, unlike the other core factors. In addition to the catalytic components, the DNA sliding clamp, PCNA (proliferating-cell nuclear antigen), plays a pivotal role in binding and co-ordinating these enzymes at sites of lagging-strand replication. Structural studies in eukaryotic and archaeal systems have revealed that PCNA-binding proteins can adopt different conformations when binding PCNA. This conformational malleability may be key to the co-ordination of these enzymes' activities.

Okazaki fragments

DNA clamp

DNA polymerase delta

Replisome

Primase

Primer (cosmetics)

DnaG

Replication factor C

DNA polymerase II

10.1042/bst0390070

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Citations (22)

Senior Chemists Committee: Examining and implementing our role

C&EN Global Enterprise (2016)

Thomas R. Beattie

In December 2015, the American Chemical Society's Senior Chemists Committee (SCC) held a strategic planning retreat in Washington, D.C. Ten SCC members, staff liaisons, and two facilitators worked for two days reviewing what we have accomplished in our first three years of existence, what we want to do in the future, and how to best achieve that. As the newest of the ACS national committees, SCC wanted to validate what we have been doing and to make certain that our upcoming plans are achievable with the resources available and consistent with the ACS Strategic Plan. The outcome of the process resulted in the creation of a strategic plan with vision and mission statements, focused goals and strategies, and a road map for implementation with project champions identified. So, what have we accomplished and where are we going? Our most direct vehicle for two-way communication has been the "Newsletter for Senior

10.1021/cen-09423-comment

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C32-amino derivatives of the immunosuppressant ascomycin

Bioorganic & Medicinal Chemistry Letters (1997)

Hyun Ok John Szumiloski Thomas R. Beattie Mark T. Goulet Mary Jo Staruch

10.1016/s0960-894x(97)00409-5

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Citations (7)