Anna Marie Pyle

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Anna Marie Pyle
Alma materPrinceton University, Columbia University
Scientific career
InstitutionsYale University, University of Colorado

Anna Marie Pyle is an American academic who is a Sterling Professor of Molecular, Cellular & Developmental Biology and a Professor of Chemistry at Yale University. and an Investigator for Howard Hughes Medical Institute. [1] Pyle is the president of the RNA Society, [2] the vice-chair of the Science and Technology Steering Committee at Brookhaven National Laboratory, and previously she served as chair of the Macromolecular Structure and Function A Study Section [3] at the National Institutes of Health.

Contents

Early life and education

Pyle grew up in Albuquerque, New Mexico, and it was there that she first became interested in science. [4] But it wasn't until after earning her bachelor's degree from Princeton University that she committed to a career in chemistry. [4] In 1990, she graduated from Columbia University with a Ph.D. in chemistry. Pyle went on to postdoc at the University of Colorado until in 1992 she established a research group at Columbia University Medical Center in the Department of Biochemistry and Molecular Biophysics. In 2002, she moved to Yale University. [1]

Research

Pyle joined Yale University in 2002. She researches the architectural features of large RNA molecules and RNA remodeling enzymes using experimental biochemistry and crystallography. such as self-splicing introns and other noncoding RNAs. She has focused her research to understand how large RNAs assemble into specific, stable tertiary structures, and also how ATP-dependent enzymes in the cell recognize and remodel RNA. Specifically, she was successful in crystallizing and solving the structure of a group IIC intron from the bacterium Oceanobacillus iheyensis [5] and moves through the stages of splicing. [6] Pyle's research may be helpful in drug development as RNA's tertiary structure could provide insight into druggable biomolecules. [7] [8]

Selected awards and honors

Related Research Articles

<span class="mw-page-title-main">Exon</span> A region of a transcribed gene present in the final functional mRNA molecule

An exon is any part of a gene that will form a part of the final mature RNA produced by that gene after introns have been removed by RNA splicing. The term exon refers to both the DNA sequence within a gene and to the corresponding sequence in RNA transcripts. In RNA splicing, introns are removed and exons are covalently joined to one another as part of generating the mature RNA. Just as the entire set of genes for a species constitutes the genome, the entire set of exons constitutes the exome.

<span class="mw-page-title-main">RNA</span> Family of large biological molecules

Ribonucleic acid (RNA) is a polymeric molecule essential in various biological roles in coding, decoding, regulation and expression of genes. RNA and deoxyribonucleic acid (DNA) are nucleic acids. Along with lipids, proteins, and carbohydrates, nucleic acids constitute one of the four major macromolecules essential for all known forms of life. Like DNA, RNA is assembled as a chain of nucleotides, but unlike DNA, RNA is found in nature as a single strand folded onto itself, rather than a paired double strand. Cellular organisms use messenger RNA (mRNA) to convey genetic information that directs synthesis of specific proteins. Many viruses encode their genetic information using an RNA genome.

<span class="mw-page-title-main">RNA splicing</span> Process in molecular biology

RNA splicing is a process in molecular biology where a newly-made precursor messenger RNA (pre-mRNA) transcript is transformed into a mature messenger RNA (mRNA). It works by removing all the introns and splicing back together exons. For nuclear-encoded genes, splicing occurs in the nucleus either during or immediately after transcription. For those eukaryotic genes that contain introns, splicing is usually needed to create an mRNA molecule that can be translated into protein. For many eukaryotic introns, splicing occurs in a series of reactions which are catalyzed by the spliceosome, a complex of small nuclear ribonucleoproteins (snRNPs). There exist self-splicing introns, that is, ribozymes that can catalyze their own excision from their parent RNA molecule. The process of transcription, splicing and translation is called gene expression, the central dogma of molecular biology.

<span class="mw-page-title-main">Alternative splicing</span> Process by which a gene can code for multiple proteins

Alternative splicing, or alternative RNA splicing, or differential splicing, is an alternative splicing process during gene expression that allows a single gene to code for multiple proteins. In this process, particular exons of a gene may be included within or excluded from the final, processed messenger RNA (mRNA) produced from that gene. This means the exons are joined in different combinations, leading to different (alternative) mRNA strands. Consequently, the proteins translated from alternatively spliced mRNAs usually contain differences in their amino acid sequence and, often, in their biological functions.

<span class="mw-page-title-main">Spliceosome</span> Molecular machine that removes intron RNA from the primary transcript

A spliceosome is a large ribonucleoprotein (RNP) complex found primarily within the nucleus of eukaryotic cells. The spliceosome is assembled from small nuclear RNAs (snRNA) and numerous proteins. Small nuclear RNA (snRNA) molecules bind to specific proteins to form a small nuclear ribonucleoprotein complex, which in turn combines with other snRNPs to form a large ribonucleoprotein complex called a spliceosome. The spliceosome removes introns from a transcribed pre-mRNA, a type of primary transcript. This process is generally referred to as splicing. An analogy is a film editor, who selectively cuts out irrelevant or incorrect material from the initial film and sends the cleaned-up version to the director for the final cut.

<span class="mw-page-title-main">Protein isoform</span> Forms of a protein produced from different genes

A protein isoform, or "protein variant", is a member of a set of highly similar proteins that originate from a single gene or gene family and are the result of genetic differences. While many perform the same or similar biological roles, some isoforms have unique functions. A set of protein isoforms may be formed from alternative splicings, variable promoter usage, or other post-transcriptional modifications of a single gene; post-translational modifications are generally not considered. Through RNA splicing mechanisms, mRNA has the ability to select different protein-coding segments (exons) of a gene, or even different parts of exons from RNA to form different mRNA sequences. Each unique sequence produces a specific form of a protein.

Small nuclear RNA (snRNA) is a class of small RNA molecules that are found within the splicing speckles and Cajal bodies of the cell nucleus in eukaryotic cells. The length of an average snRNA is approximately 150 nucleotides. They are transcribed by either RNA polymerase II or RNA polymerase III. Their primary function is in the processing of pre-messenger RNA (hnRNA) in the nucleus. They have also been shown to aid in the regulation of transcription factors or RNA polymerase II, and maintaining the telomeres.

<span class="mw-page-title-main">Group II intron</span> Class of self-catalyzing ribozymes

Group II introns are a large class of self-catalytic ribozymes and mobile genetic elements found within the genes of all three domains of life. Ribozyme activity can occur under high-salt conditions in vitro. However, assistance from proteins is required for in vivo splicing. In contrast to group I introns, intron excision occurs in the absence of GTP and involves the formation of a lariat, with an A-residue branchpoint strongly resembling that found in lariats formed during splicing of nuclear pre-mRNA. It is hypothesized that pre-mRNA splicing may have evolved from group II introns, due to the similar catalytic mechanism as well as the structural similarity of the Group II Domain V substructure to the U6/U2 extended snRNA. Finally, their ability to site-specifically insert into DNA sites has been exploited as a tool for biotechnology. For example, group II introns can be modified to make site-specific genome insertions and deliver cargo DNA such as reporter genes or lox sites

<span class="mw-page-title-main">Joan A. Steitz</span> American biochemist

Joan Elaine Argetsinger Steitz is Sterling Professor of Molecular Biophysics and Biochemistry at Yale University and Investigator at the Howard Hughes Medical Institute. She is known for her discoveries involving RNA, including ground-breaking insights into how ribosomes interact with messenger RNA by complementary base pairing and that introns are spliced by small nuclear ribonucleic proteins (snRNPs), which occur in eukaryotes. In September 2018, Steitz won the Lasker-Koshland Award for Special Achievement in Medical Science. The Lasker award is often referred to as the 'American Nobel' because 87 of the former recipients have gone on to win Nobel prizes.

<span class="mw-page-title-main">U6 spliceosomal RNA</span>

U6 snRNA is the non-coding small nuclear RNA (snRNA) component of U6 snRNP, an RNA-protein complex that combines with other snRNPs, unmodified pre-mRNA, and various other proteins to assemble a spliceosome, a large RNA-protein molecular complex that catalyzes the excision of introns from pre-mRNA. Splicing, or the removal of introns, is a major aspect of post-transcriptional modification and takes place only in the nucleus of eukaryotes.

<span class="mw-page-title-main">RBFOX1</span> Protein-coding gene in the species Homo sapiens

Fox-1 homolog A, also known as ataxin 2-binding protein 1 (A2BP1) or hexaribonucleotide-binding protein 1 (HRNBP1) or RNA binding protein, fox-1 homolog (Rbfox1), is a protein that in humans is encoded by the RBFOX1 gene.

<span class="mw-page-title-main">Thomas A. Steitz</span> American biochemist (1940–2018)

Thomas Arthur Steitz was an American biochemist, a Sterling Professor of Molecular Biophysics and Biochemistry at Yale University, and investigator at the Howard Hughes Medical Institute, best known for his pioneering work on the ribosome.

<span class="mw-page-title-main">Nucleic acid tertiary structure</span> Three-dimensional shape of a nucleic acid polymer

Nucleic acid tertiary structure is the three-dimensional shape of a nucleic acid polymer. RNA and DNA molecules are capable of diverse functions ranging from molecular recognition to catalysis. Such functions require a precise three-dimensional structure. While such structures are diverse and seemingly complex, they are composed of recurring, easily recognizable tertiary structural motifs that serve as molecular building blocks. Some of the most common motifs for RNA and DNA tertiary structure are described below, but this information is based on a limited number of solved structures. Many more tertiary structural motifs will be revealed as new RNA and DNA molecules are structurally characterized.

Numerous key discoveries in biology have emerged from studies of RNA, including seminal work in the fields of biochemistry, genetics, microbiology, molecular biology, molecular evolution and structural biology. As of 2010, 30 scientists have been awarded Nobel Prizes for experimental work that includes studies of RNA. Specific discoveries of high biological significance are discussed in this article.

Alanna Schepartz is an American professor and scientist. She is currently the T.Z. and Irmgard Chu Distinguished Chair in Chemistry at University of California, Berkeley. She was formerly the Sterling Professor of Chemistry at Yale University.

Scott A. Strobel is the provost, Henry Ford II professor of molecular biophysics and biochemistry, and a professor of chemistry at Yale University. He was the vice provost for Science Initiatives and vice president for West Campus Planning & Program Development. An educator and researcher, he has led a number of Yale initiatives over the past two decades. Strobel was appointed as Yale's provost in 2020.

Oceanobacillus iheyensis is a bacterium, the type species of its genus. It is a deep-sea species, having been isolated from a depth of 1,050 metres (3,440 ft), and is extremely halotolerant and alkaliphilic. Its type strain is HTE831. Oceanobacillus iheyensis HTE831 is an alkaliphilic and extremely halotolerant Bacillus-related species isolated from deep-sea sediment.

<span class="mw-page-title-main">R-loop</span> Three-stranded nucleic acid structure

An R-loop is a three-stranded nucleic acid structure, composed of a DNA:RNA hybrid and the associated non-template single-stranded DNA. R-loops may be formed in a variety of circumstances, and may be tolerated or cleared by cellular components. The term "R-loop" was given to reflect the similarity of these structures to D-loops; the "R" in this case represents the involvement of an RNA moiety.

Susan A. Martinis is an American biochemist. She has co-authored over 57 publications in peer reviewed journals and scientific book chapters. Her expertise is in protein:RNA interactions and aminoacyl tRNA synthetases. As of 2019, she is the Vice Chancellor for Research and Innovation at the University of Illinois at Urbana-Champaign.

<span class="mw-page-title-main">Alan Lambowitz</span> American academic

Alan Lambowitz is a professor for the University of Texas at Austin in Molecular Biosciences and Oncology and has been instrumental in many bio-molecular processes and concepts, such as intron splicing and mitochondrial ribosomal assembly.

References

  1. 1 2 "Anna Marie Pyle, Ph.D. | Molecular, Cellular and Developmental Biology". mcdb.yale.edu. Retrieved 2019-03-01.
  2. ↑ "RNA Society" . Retrieved 2019-03-01.
  3. ↑ "MSFA | NIH Center for Scientific Review". public.csr.nih.gov. Retrieved 2019-03-01.
  4. 1 2 "2016 Annual Meeting Plenary Lecturer: Pyle". www.asbmb.org. Retrieved 2019-03-01.
  5. ↑ Toor, Navtej; Keating, Kevin S.; Fedorova, Olga; Rajashankar, Kanagalaghatta; Wang, Jimin; Pyle, Anna Marie (January 2010). "Tertiary architecture of the Oceanobacillus iheyensis group II intron". RNA. 16 (1): 57–69. doi:10.1261/rna.1844010. ISSN   1355-8382. PMC   2802037 . PMID   19952115.
  6. ↑ Pyle, A. M.; Marcia, M. (2012). "Visualizing Group II Intron Catalysis through the Stages of Splicing". Cell. 151 (3): 497–507. doi:10.2210/pdb4e8k/pdb. PMC   3628766 . PMID   23101623.
  7. ↑ "Targeting RNA's tertiary structure". Chemical & Engineering News. Retrieved 2019-03-01.
  8. ↑ Pyle, Anna Marie; Zandt, Michael C. Van; Lin Yuan; Adams, Rebecca L.; Jagdmann, G. Erik; Fedorova, Olga (December 2018). "Small molecules that target group II introns are potent antifungal agents". Nature Chemical Biology. 14 (12): 1073–1078. doi:10.1038/s41589-018-0142-0. ISSN   1552-4469. PMC   6239893 . PMID   30323219.
  9. ↑ "2023 NAS Election". National Academy of Sciences. 2023-05-02. Retrieved 2023-05-02.
  10. ↑ "Anna Marie Pyle appointed Sterling Professor". YaleNews. 2018-07-19. Retrieved 2019-03-01.
  11. ↑ "Historic Fellows". American Association for the Advancement of Science. Retrieved 2019-03-01.
  12. ↑ "Anna Marie Pyle". American Academy of Arts & Sciences. Retrieved 2019-03-01.
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