Squire Booker

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Squire Booker
BookerSquire.jpg
BornSeptember 9, 1965
Beaumont, Texas
Alma materB.A. in Chemistry at Austin College (1987)

Ph.D. in Biochemistry at Massachusetts Institute of Technology (1994)
NSF-NATO Postdoctoral Fellow (1994-1995)

NIH Postdoctoral Fellow at the Institute for Enzyme Research at the University of Wisconsin (1996-1999)

Contents

Known forBiochemistry research with iron-sulfur clusters enzymes
AwardsPresidential Early Career Award in Science and Engineering (2004)

American Chemical Society Arthur C. Cope Scholar Award (2011)
Howard Hughes Medical Institute Investigator (2015)

Associate Editor for the American Chemical Society Biochemistry Journal (2019)
Scientific career
InstitutionsPenn State University (1999-Present)

Squire Booker is an American biochemist at Penn State University. [1] Booker directs an interdisciplinary chemistry research program related to fields of biochemistry, enzymology, protein chemistry, natural product biosynthesis, and mechanisms of radical dependent enzymes. [1] [2] He is an associate editor for the American Chemical Society Biochemistry Journal, [2] is a Hughes Medical Institute Investigator, [1] [2] [3] and an Eberly Distinguished Chair in Science at Penn State University. [1] [4]

Early life

Booker was born September 9, 1965. He grew up in the segregated community of Beaumont, Texas. He was raised by his grandmother with the help of three uncles. [5] [6] [7] Squire Booker's career was particularly influenced by two of his uncles. One worked at NASA and sparked his interest in astronomy, while the other was a math teacher who inspired his curiosity for solving complex problems. This led him to choose chemistry as his major in college, which combined his interests in math and science. [8]

Education

Booker received his B.A. in chemistry at Austin College in 1987, [1] where he was a Minnie Stevens Piper Scholar. [9] He received his Ph.D. in biochemistry from Massachusetts Institute of Technology in 1994, [1] and conducted postdoctoral research at Universite Rene Decartes in Paris, France and held a postdoctoral fellowship at the Institute for Enzyme Research at the University of Wisconsin. He became a professor at Penn State University in 1999, [10] where he earned tenure in 2005. [11]

Research

Booker is a professor of biology, biochemistry, and molecular biology at Penn State University. [1] [2] His research explores how enzymes change their catalytic abilities due to metal ions or metal clusters. [12] [13] His research focuses on enzymes containing iron-sulfur clusters which catalyze chemical reactions. [1] [14] [15] He focuses on the Radical S-adenosylamethionine Superfamily (SAM) which is a group of enzymes that encounters radical chemistry in post-transcriptional and post-translational modifications of DNA. [1] [16] [17] [18]

He also researches many bacteria including Staphylococcus aureus , which is found in the nasal cavity and on the skin in humans. [19] S. aureus is problematic because it can mutate into the superbug methicillin-resistant S. aureus (MRSA). [20] There is a protein called Cfr protein in S. aureus that binds to ribosomes which is where translation occurs. Many antibiotics bind to ribosomes which cause bacteria to die. However, when Cfr is expressed, it binds to the ribosome and allows the bacteria to stay alive which is known as methylation [21] [22] [23]

This research has led Booker to discover that S. aureus expresses a protein, Cfr, which makes it resistant to many antibiotics. [24] He developed mechanism of this methylation. [25] [26] Booker's lab also researches aspects of the bacterium, Escherichia coli . [27] [28] [29] He determined the three-dimensional structure of the RImN protein from the bacteria. RImN is one of two proteins which makes chemical modification to different RNA molecules. Understanding this structure will help with other research of antibiotic resistance. [30] [31] As a result of his research, he is synthesizing new compounds to stop the bacteria's defenses which would make antibiotics more effective. [2] [32] The goal of his research to design compounds which can prevent infections due to drug-resistant bacteria. [32] [33]

Activism

Booker is active in promoting diversity in Science, Technology, Engineering, and Mathematics (STEM) especially towards undergraduate and graduate students. He was a chair on the Minority Affairs Committee of the American Association of Biochemistry and Molecular Biology. [9] In 2010, he helped organize a workshop which discussed the different obstacles and challenges that minorities in biochemistry and molecular biology encounter when building externally funded research programs. [34] [35]

Booker was the guest speaker at Massachusetts Institute of Technology's 2019 Investiture of Doctoral Hoods and Degree Conferral Ceremony. [6] He was chosen due to his impressive contributions to the scientific community and his activism towards inclusion of all in STEM. In his speech, he emphasized an opportunity for all in science. [5] He encouraged the graduates to take responsibility and give back to society. It does not matter what one's background is in, people in STEM need to be willing to accept and stand up for each other. [7] [6]

Honors and awards

Booker has received numerous honor and awards:

Selected publications

Booker has published over 100 scientific publications in journals such as the Journal of the American Chemical Society and Proceedings of the National Academy of Sciences. [9] Here are some of the most cited publications:

Related Research Articles

<span class="mw-page-title-main">Hypochlorous acid</span> Chemical compound

Hypochlorous acid is an inorganic compound with the chemical formula ClOH, also written as HClO, HOCl, or ClHO. Its structure is H−O−Cl. It is an acid that forms when chlorine dissolves in water, and itself partially dissociates, forming hypochlorite anion, ClO−. HClO and ClO− are oxidizers, and the primary disinfection agents of chlorine solutions. HClO cannot be isolated from these solutions due to rapid equilibration with its precursor, chlorine.

<i>S</i>-Adenosyl methionine Chemical compound found in all domains of life with largely unexplored effects

S-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throughout the body, most SAM is produced and consumed in the liver. More than 40 methyl transfers from SAM are known, to various substrates such as nucleic acids, proteins, lipids and secondary metabolites. It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase. SAM was first discovered by Giulio Cantoni in 1952.

Iron–sulfur proteins are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins, such as the ferredoxins, as well as NADH dehydrogenase, hydrogenases, coenzyme Q – cytochrome c reductase, succinate – coenzyme Q reductase and nitrogenase. Iron–sulfur clusters are best known for their role in the oxidation-reduction reactions of electron transport in mitochondria and chloroplasts. Both Complex I and Complex II of oxidative phosphorylation have multiple Fe–S clusters. They have many other functions including catalysis as illustrated by aconitase, generation of radicals as illustrated by SAM-dependent enzymes, and as sulfur donors in the biosynthesis of lipoic acid and biotin. Additionally, some Fe–S proteins regulate gene expression. Fe–S proteins are vulnerable to attack by biogenic nitric oxide, forming dinitrosyl iron complexes. In most Fe–S proteins, the terminal ligands on Fe are thiolate, but exceptions exist.

<span class="mw-page-title-main">Methionine synthase</span> Mammalian protein found in Homo sapiens

Methionine synthase (MS, MeSe, MTR) is responsible for the regeneration of methionine from homocysteine. In humans it is encoded by the MTR gene (5-methyltetrahydrofolate-homocysteine methyltransferase). Methionine synthase forms part of the S-adenosylmethionine (SAMe) biosynthesis and regeneration cycle, and is the enzyme responsible for linking the cycle to one-carbon metabolism via the folate cycle. There are two primary forms of this enzyme, the Vitamin B12 (cobalamin)-dependent (MetH) and independent (MetE) forms, although minimal core methionine synthases that do not fit cleanly into either category have also been described in some anaerobic bacteria. The two dominant forms of the enzymes appear to be evolutionary independent and rely on considerably different chemical mechanisms. Mammals and other higher eukaryotes express only the cobalamin-dependent form. In contrast, the distribution of the two forms in Archaeplastida (plants and algae) is more complex. Plants exclusively possess the cobalamin-independent form, while algae have either one of the two, depending on species. Many different microorganisms express both the cobalamin-dependent and cobalamin-independent forms.

<span class="mw-page-title-main">Biotin synthase</span> Enzyme

Biotin synthase (BioB) is an enzyme that catalyzes the conversion of dethiobiotin (DTB) to biotin; this is the final step in the biotin biosynthetic pathway. Biotin, also known as vitamin B7, is a cofactor used in carboxylation, decarboxylation, and transcarboxylation reactions in many organisms including humans. Biotin synthase is an S-Adenosylmethionine (SAM) dependent enzyme that employs a radical mechanism to thiolate dethiobiotin, thus converting it to biotin.

<span class="mw-page-title-main">Malate synthase</span> Class of enzymes

In enzymology, a malate synthase (EC 2.3.3.9) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Dipeptidase 1</span> Protein-coding gene in the species Homo sapiens

Dipeptidase 1 (DPEP1), or renal dipeptidase, is a membrane-bound glycoprotein responsible for hydrolyzing dipeptides. It is found in the microsomal fraction of the porcine kidney cortex. It exists as a disulfide-linked homodimer that is glygosylphosphatidylinositol (GPI)-anchored to the renal brush border of the kidney. The active site on each homodimer is made up of a barrel subunit with binuclear zinc ions that are bridged by the Gly125 side-chain located at the bottom of the barrel.

<span class="mw-page-title-main">Stephen J. Benkovic</span> American chemist

Stephen James Benkovic is an American chemist known for his contributions to the field of enzymology. He holds the Evan Pugh University Professorship and Eberly Chair in Chemistry at The Pennsylvania State University. He has developed boron compounds that are active pharmacophores against a variety of diseases. Benkovic has concentrated on the assembly and kinetic attributes of the enzymatic machinery that performs DNA replication, DNA repair, and purine biosynthesis.

Radical SAMenzymes is a superfamily of enzymes that use a [4Fe-4S]+ cluster to reductively cleave S-adenosyl-L-methionine (SAM) to generate a radical, usually a 5′-deoxyadenosyl radical (5'-dAdo), as a critical intermediate. These enzymes utilize this radical intermediate to perform diverse transformations, often to functionalize unactivated C-H bonds. Radical SAM enzymes are involved in cofactor biosynthesis, enzyme activation, peptide modification, post-transcriptional and post-translational modifications, metalloprotein cluster formation, tRNA modification, lipid metabolism, biosynthesis of antibiotics and natural products etc. The vast majority of known radical SAM enzymes belong to the radical SAM superfamily, and have a cysteine-rich motif that matches or resembles CxxxCxxC. Radical SAM enzymes comprise the largest superfamily of metal-containing enzymes.

23S rRNA (adenine2503-C2)-methyltransferase (EC 2.1.1.192, RlmN, YfgB, Cfr) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C2)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenine2503-C8)-methyltransferase (EC 2.1.1.224, Cfr (gene)) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2503-C8)-methyltransferase. This enzyme catalyses the following chemical reaction

S-Adenosylmethionine:tRNA ribosyltransferase-isomerase is an enzyme with systematic name S-adenosyl-L-methionine:7-aminomethyl-7-deazaguanosine ribosyltransferase . This enzyme catalyses the following chemical reaction

Cyclic pyranopterin monophosphate synthase is an enzyme with systematic name GTP 8,9-lyase . This enzyme catalyses the following chemical reaction

tRNA pseudouridine32 synthase is an enzyme with systematic name tRNA-uridine32 uracil mutase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Dehydroamino acid</span>

In biochemistry, a dehydroamino acid or α,β-dehydroamino acid is an amino acids, usually with a C=C double bond in its side chain. Dehydroamino acids are not coded by DNA, but arise via post-translational modification.

Alice Vrielink is a structural biologist and Professor of Structural Biology in the School of Molecular Sciences at the University of Western Australia. She is known for her work determining the structures of macromolecules such as enzymes and nucleic acids.

Joan Blanchette Broderick is a professor of chemistry and biochemistry at Montana State University known for her work on bioinorganic chemistry, especially the chemistry of iron-sulfur interactions. She was elected a member of the National Academy of Sciences in 2022.

Methylthiotransferases are enzymes of the radical S-adenosyl methionine superfamily. These enzymes catalyze the addition of a methylthio group to various biochemical compounds including tRNA and proteins. Methylthiotransferases are classified into one of four classes based on their substrates and mechanisms. All methylthiotransferases have been shown to contain two Fe-S clusters, one canonical cluster and one auxiliary cluster, that both function in the addition of the methylthio group to the substrate.

R. David Britt is the Winston Ko Chair and Distinguished Professor of Chemistry at the University of California, Davis. Britt uses electron paramagnetic resonance (EPR) spectroscopy to study metalloenzymes and enzymes containing organic radicals in their active sites. Britt is the recipient of multiple awards for his research, including the Bioinorganic Chemistry Award in 2019 and the Bruker Prize in 2015 from the Royal Society of Chemistry. He has received a Gold Medal from the International EPR Society (2014), and the Zavoisky Award from the Kazan Scientific Center of the Russian Academy of Sciences (2018). He is a Fellow of the American Association for the Advancement of Science and of the Royal Society of Chemistry.

Kenichi Yokoyama is an enzymologist, chemical biologist, and natural product biochemist originally from Tokyo, Japan. He is an Associate Professor of Biochemistry at Duke University School of Medicine. In 2019, Yokoyama was awarded the Pfizer Award in Enzyme Chemistry from the American Chemical Society.

References

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  2. 1 2 3 4 5 6 7 Schepartz, Alanna (2019-12-24). "Welcome New Associate Editor, Squire Booker". Biochemistry. 58 (51): 5099. doi: 10.1021/acs.biochem.9b01057 . ISSN   0006-2960. PMID   31870158.
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  13. ↑ Cicchillo, Robert M.; Iwig, David F.; Jones, A. Daniel; Nesbitt, Natasha M.; Baleanu-Gogonea, Camelia; Souder, Matthew G.; Tu, Loretta; Booker, Squire J. (June 2004). "Lipoyl Synthase Requires Two Equivalents ofS-Adenosyl-l-methionine To Synthesize One Equivalent of Lipoic Acid†". Biochemistry. 43 (21): 6378–6386. doi:10.1021/bi049528x. ISSN   0006-2960. PMID   15157071.
  14. ↑ Lieder, Kafryn W.; Booker, Squire; Ruzicka, Frank J.; Beinert, Helmut; Reed, George H.; Frey, Perry A. (February 1998). "S-Adenosylmethionine-Dependent Reduction of Lysine 2,3-Aminomutase and Observation of the Catalytically Functional Iron−Sulfur Centers by Electron Paramagnetic Resonance†". Biochemistry. 37 (8): 2578–2585. doi:10.1021/bi972417w. ISSN   0006-2960. PMID   9485408.
  15. ↑ Blaszczyk, Anthony J.; Silakov, Alexey; Zhang, Bo; Maiocco, Stephanie J.; Lanz, Nicholas D.; Kelly, Wendy L.; Elliott, Sean J.; Krebs, Carsten; Booker, Squire J. (2016-03-03). "Spectroscopic and Electrochemical Characterization of the Iron–Sulfur and Cobalamin Cofactors of TsrM, an Unusual Radical S-Adenosylmethionine Methylase". Journal of the American Chemical Society. 138 (10): 3416–3426. doi:10.1021/jacs.5b12592. ISSN   0002-7863. PMID   26841310.
  16. ↑ Grove, Tyler L.; Lee, Kyung-Hoon; St. Clair, Jennifer; Krebs, Carsten; Booker, Squire J. (July 2008). "In Vitro Characterization of AtsB, a Radical SAM Formylglycine-Generating Enzyme That Contains Three [4Fe-4S] Clusters†". Biochemistry. 47 (28): 7523–7538. doi:10.1021/bi8004297. ISSN   0006-2960. PMC   2664749 . PMID   18558715.
  17. ↑ Chatterjee, Abhishek; Li, Yue; Zhang, Yang; Grove, Tyler L; Lee, Michael; Krebs, Carsten; Booker, Squire J; Begley, Tadhg P; Ealick, Steven E (2008-10-26). "Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily". Nature Chemical Biology. 4 (12): 758–765. doi:10.1038/nchembio.121. ISSN   1552-4450. PMC   2587053 . PMID   18953358.
  18. ↑ Booker, Squire J; Cicchillo, Robert M; Grove, Tyler L (October 2007). "Self-sacrifice in radical S-adenosylmethionine proteins". Current Opinion in Chemical Biology. 11 (5): 543–552. doi:10.1016/j.cbpa.2007.08.028. ISSN   1367-5931. PMC   2637762 . PMID   17936058.
  19. ↑ Booker, S.; Stubbe, J. (1993-09-15). "Cloning, sequencing, and expression of the adenosylcobalamin-dependent ribonucleotide reductase from Lactobacillus leichmannii". Proceedings of the National Academy of Sciences. 90 (18): 8352–8356. Bibcode:1993PNAS...90.8352B. doi: 10.1073/pnas.90.18.8352 . ISSN   0027-8424. PMC   47354 . PMID   8397403.
  20. ↑ Sanders, Laura (2010-09-28). "Genes & cells: Superbug secret revealed". Science News. 178 (7): 9. doi:10.1002/scin.5591780708. ISSN   0036-8423.
  21. ↑ Peng Jiang, Peng Jiang (2015-02-10). "Sequencing the Cactus Genome to Discover the Secret of Drought Resistance". Experiment. doi:10.18258/4612.
  22. ↑ "Effective antibiotics are in sight after scientists unlock secrets of superbug". Nursing Standard. 26 (4): 17. 2011-09-28. doi:10.7748/ns.26.4.17.s23. ISSN   0029-6570.
  23. ↑ Bauerle, Matthew R.; Schwalm, Erica L.; Booker, Squire J. (2014-12-04). "Mechanistic Diversity of RadicalS-Adenosylmethionine (SAM)-dependent Methylation". Journal of Biological Chemistry. 290 (7): 3995–4002. doi: 10.1074/jbc.r114.607044 . ISSN   0021-9258. PMC   4326810 . PMID   25477520.
  24. ↑ Grove, Tyler L; Livada, Jovan; Schwalm, Erica L; Green, Michael T; Booker, Squire J; Silakov, Alexey (2013-05-05). "A substrate radical intermediate in catalysis by the antibiotic resistance protein Cfr". Nature Chemical Biology. 9 (7): 422–427. doi:10.1038/nchembio.1251. ISSN   1552-4450. PMC   3897224 . PMID   23644479.
  25. ↑ Boal, A. K.; Grove, T. L.; McLaughlin, M. I.; Yennawar, N. H.; Booker, S. J.; Rosenzweig, A. C. (2011-04-28). "Structural Basis for Methyl Transfer by a Radical SAM Enzyme". Science. 332 (6033): 1089–1092. Bibcode:2011Sci...332.1089B. doi:10.1126/science.1205358. ISSN   0036-8075. PMC   3506250 . PMID   21527678.
  26. ↑ Grove, T. L.; Benner, J. S.; Radle, M. I.; Ahlum, J. H.; Landgraf, B. J.; Krebs, C.; Booker, S. J. (2011-03-17). "A Radically Different Mechanism for S-Adenosylmethionine-Dependent Methyltransferases". Science. 332 (6029): 604–607. Bibcode:2011Sci...332..604G. doi: 10.1126/science.1200877 . ISSN   0036-8075. PMID   21415317. S2CID   2214309.
  27. ↑ Lanz, Nicholas D.; Blaszczyk, Anthony J.; McCarthy, Erin L.; Wang, Bo; Wang, Roy X.; Jones, Brianne S.; Booker, Squire J. (2018-01-03). "Enhanced Solubilization of Class B Radical S-Adenosylmethionine Methylases by Improved Cobalamin Uptake in Escherichia coli". Biochemistry. 57 (9): 1475–1490. doi:10.1021/acs.biochem.7b01205. ISSN   0006-2960. PMC   5941297 . PMID   29298049.
  28. ↑ McCarthy, Erin L.; Booker, Squire J. (2018), "Biochemical Approaches for Understanding Iron–Sulfur Cluster Regeneration in Escherichia coli Lipoyl Synthase During Catalysis", Radical SAM Enzymes, Methods in Enzymology, vol. 606, Elsevier, pp. 217–239, doi:10.1016/bs.mie.2018.06.006, ISBN   978-0-12-812794-0, PMC   6501195 , PMID   30097094
  29. ↑ Cicchillo, Robert M.; Lee, Kyung-Hoon; Baleanu-Gogonea, Camelia; Nesbitt, Natasha M.; Krebs, Carsten; Booker, Squire J. (September 2004). "Escherichia coli Lipoyl Synthase Binds Two Distinct [4Fe−4S] Clusters per Polypeptide†". Biochemistry. 43 (37): 11770–11781. doi:10.1021/bi0488505. ISSN   0006-2960. PMID   15362861.
  30. ↑ Pennisi, E. (1993-05-22). "Cancer Cells Caught in the (Metastatic) Act". Science News. 143 (21): 324. doi:10.2307/3977284. ISSN   0036-8423. JSTOR   3977284.
  31. ↑ McCarthy, Erin L.; Rankin, Ananda N.; Dill, Zerick R.; Booker, Squire J. (2018-12-11). "The A-type domain in Escherichia coli NfuA is required for regenerating the auxiliary [4Fe–4S] cluster in Escherichia coli lipoyl synthase". Journal of Biological Chemistry. 294 (5): 1609–1617. doi: 10.1074/jbc.ra118.006171 . ISSN   0021-9258. PMC   6364782 . PMID   30538130.
  32. 1 2 ARNAUD, CELIA (2007-08-13). "Novel Antibiotic Mechanism". Chemical & Engineering News. 85 (33): 13. doi:10.1021/cen-v085n033.p013a. ISSN   0009-2347.
  33. ↑ Rajakovich, Lauren J.; Nørgaard, Hanne; Warui, Douglas M.; Chang, Wei-chen; Li, Ning; Booker, Squire J.; Krebs, Carsten; Bollinger, J. Martin; Pandelia, Maria-Eirini (2015-09-02). "Rapid Reduction of the Diferric-Peroxyhemiacetal Intermediate in Aldehyde-Deformylating Oxygenase by a Cyanobacterial Ferredoxin: Evidence for a Free-Radical Mechanism". Journal of the American Chemical Society. 137 (36): 11695–11709. doi:10.1021/jacs.5b06345. ISSN   0002-7863. PMID   26284355.
  34. 1 2 "NSF Outreach Service". Anthropology News. 26 (4): 13. April 1985. doi:10.1111/an.1985.26.4.13.4. ISSN   1541-6151.
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  37. ↑ "ACS News". Chemical & Engineering News. 56 (25): 38–39. 1978-06-19. doi: 10.1021/cen-v056n025.p038 . ISSN   0009-2347.
  38. ↑ "Psychologist Steven Breckler named fellow of American Association for the Advancement of Science". 2008. doi:10.1037/e539992008-001.{{cite journal}}: Cite journal requires |journal= (help)
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