Forster Lab

From OpenWetWare
Jump to navigationJump to search
Minimal Cell Project
Minimal Cell Project

The Boss!?

Professor Anthony C. Forster, M.D., Ph.D.
Program in Molecular Biology
Department of Cell and Molecular Biology
Uppsala University

office and mailing address:
ICM Dept., Room D9:216b
Husargatan 3, Box 596
75124 Uppsala, Sweden

office and cell phone: +46-18-471 4618
e-mail: a.forster(at)
lab web:
Department web:
Uppsala University web:

Anthony C. Forster (Ph.D. Biochem., U. Adelaide; M.D., Harvard U.) researches RNA, protein synthesis and applications thereof (synthetic biology). He discovered the hammerhead catalytic RNA structure, invented external guide sequences for ribonuclease P, and created unnatural genetic codes de novo, all of which founded biotech companies. He has published in journals including Cell, Nature and Science, edited volumes of Methods and Biotechnology J., and coauthored "Synthetic Biology: A Lab Manual."

Research Description:
Synthetic biology and protein synthesis
SynBio is a creative new field defined as the complex engineering of replicating systems. It encompasses next-generation technology for bioengineering and fresh approaches to global challenges such as drug discovery and biofuels.
Our current projects include:
1. Improving ribosomal incorporation of unnatural amino acids for investigating translation mechanism and for applications such as directed evolution of peptidomimetic drugs.
2. Development of chromoproteins as reporters and for biosensor diagnostics.
3. Understanding and improving transcription termination.
4. Improving vaccines via synthetic biology.
5. Determining functions of ribosomal RNA modifications towards synthesis of the ribosome and self-replication.

Research Keywords:
Synthetic biology, protein synthesis, drug discovery, transcription termination, chromoprotein, fluorescent protein, unnatural amino acid, directed evolution, translation, ribosome, RNA, modification enzyme, E. coli, bacteria, microbiology, biochemistry, vaccine, Tony Forster

Meet our lab group:

Minimal Cell Project
Minimal Cell Project

phones in lab:
+46-18-471 4387, 471 4651 and 471 4204

1MB433: Synthetic Biology (10 hp, weeks 4-9)
1BG044: Frontiers in Bioscience (10 hp, weeks 37-51)
1MB205 and 1MB405 Project in laboratory synthetic biology I and II (Uppsala iGEM) courses, co-director
iGEM 2020 Uppsala University Team Members:
Congratulations on winning "Best new application" prize!
iGEM 2014 Ravenwood High School Team Members:
Congratulations on being the first iGEM team from Tennessee!

Postdoctoral Applicants:
Minimal qualifications include expertise in molecular biology and 2 first-authored research papers in international peer-reviewed journals. Experience with bacterial translation or RNA is a plus. Please mail a letter of interest and C.V.

Master and PhD Applicants:
Students enrolled in a Master program (including EU students seeking an Erasmus exchange) are welcome to apply for a few months' work experience in the lab. Most students achieve authorship on a publication, and extension into a PhD position is possible. Research experience is a plus. Please mail a letter of interest and C.V.

Forster, A C, Blacklow, S C. Process and compositions for peptide, protein and peptidomimetic synthesis. US6977150
(founding I.P. for Ra Pharmaceuticals, Inc., Boston, now merged with UCB).
Altman, S, Forster, A C, Guerrier-Takada, C L. Cleavage of targeted RNA by RNAase P. US5168053
(founding I.P. for Innovir Laboratories, Inc., NY).

Almost all pubs indexed by and available from PubMed: (type "Forster AC")
Citations per paper are available from Google Scholar: (type "Forster AC")

Bao, L, Karpenko, V V, Forster, A C. Rate-limiting hydrolysis in ribosomal release reactions revealed by ester activation. J. Biol. Chem., 298, 102509, 1-9, 2022
Open access:

Forster, A C. Tales of the unexpected in Sidney Altman's laboratory. RNA, 28, 1406-1408, 2022
Open access: doi: 10.1261/rna.079397.122

Liljeruhm, J, Leppik, M, Bao, L, Truu, T, Calvo-Noriega, M, Freyer, N S, Liiv, A, Wang, J, Crespo Blanco, R, Ero,
 R, Remme, J, Forster, A C. Plasticity and conditional essentiality of modification enzymes for domain V of Escherichia coli 23S ribosomal RNA. RNA, 28, 796-807, 2022
doi: 10.1261/rna.079096.121

Forster, A C. Revisiting the extinction of the RNA world. Biochemistry, 61, 749-751, 2022
Open access

Doerr, A, Foschepoth, D, Forster, A C, Danelon, C. In vitro synthesis of 32 translation-factor proteins from a single template reveals impaired ribosomal processivity. Sci. Rep. 11:1898, 1-12, 2021
Open access

Bao, L, Menon, P N K, Liljeruhm, J, Forster, A C. Overcoming chromoprotein limitations by engineering a red fluorescent protein. Anal. Biochem. 611:113936, 1-8, 2020
Open access

Vogel, C, Gynnå, A, Yuan, J, Bao, L, Liljeruhm, J, Forster, A C. Rationally-designed Spot 42 RNAs with an inhibition/toxicity profile advantageous for engineering E. coli. Engineering Rep., 2:3, e12126, 1-10, 2020
Our front cover and open access:

Liljeruhm, J, Wang, J, Kwiatkowski, M, Sabari, S, Forster, A C. Kinetics of D-amino acid incorporation in translation. ACS Chem. Biol. 14:204-213, 2019
Open access:

Wang, J, Forster, A C. Ribosomal incorporation of unnatural amino acids: lessons and improvements from fast kinetics studies. Curr. Opin. Chem. Biol. 46:180-187, 2018
Open access:

Liljeruhm, J, Funk, S K, Tietscher, S, Edlund, A D, Jamal, S, Wistrand-Yuen, P, Dyrhage, K, Gynnå, A, Ivermark, K, Lövgren, J, Törnblom, V, Virtanen, A, Lundin, E R, Wistrand-Yuen, E, Forster, A C. Engineering a palette of eukaryotic chromoproteins for bacterial synthetic biology. J. Biol. Eng. 12:8, 1-10, 2018

Shepherd, T R, Du, L, Liljeruhm, J, Samudyata, Wang, J, Sjödin, M O D, Wetterhall, M, Yomo, T, Forster, A C. De novo design and synthesis of a 30-cistron translation-factor module. Nucleic Acids Res. 45, 10895-10905, 2017

Wang, J, Forster, A C. Translational roles of the C75 2'OH in an in vitro tRNA transcript at the ribosomal A, P and E sites. Sci. Rep. 7, 6709, 1-8, 2017

Wang, J, Kwiatkowski, M, Forster, A C. Ribosomal peptide syntheses from activated substrates reveal rate limitation by an unexpected step at the peptidyl site. J. Am. Chem. Soc. 138, 15587-15595, 2016

Wang, J, Kwiatkowski, M, Forster, A C. Kinetics of tRNAPyl-mediated amber suppression in E. coli translation reveals unexpected limiting steps and competing reactions. Biotechnol. Bioeng. 113, 1552-1559, 2016

Wang, J, Kwiatkowski, M, Forster, A C. Kinetics of ribosome-catalyzed polymerization using artificial aminoacyl-tRNA substrates clarifies inefficiencies and improvements. ACS Chem. Biol. 10, 2187-2192, 2015

Kwiatkowski, M, Wang, J, Forster, A C. Facile synthesis of N-acyl-aminoacyl-pCpA for preparation of mischarged fully ribo tRNA. Bioconjugate Chem. 25, 2086-2091, 2014

Liljeruhm, J, Gullberg, E, Forster A C. Synthetic biology: A lab manual. World Scientific Press, 204 pp, 2014

Wang, J, Kwiatkowski, M, Pavlov, M Y, Ehrenberg, M, Forster, A C. Peptide formation by N-methyl amino acids in translation is hastened by higher pH and tRNAPro. ACS Chem. Biol. 9, 1303-1311 and front cover, 2014

Ieong, K-W, Pavlov, M Y, Kwiatkowski, M, Ehrenberg, M, Forster, A C. A tRNA body with high affinity for EF-Tu hastens ribosomal incorporation of unnatural amino acids. RNA 20, 632-643, 2014

Punekar, A, Liljeruhm, J, Shepherd, T R, Forster, A C, Selmer, M. Structural and functional insights into the molecular mechanism of rRNA m6A methyltransferase RlmJ. Nucleic Acids Res. 41, 9537-9548, 2013

Quax, T E F, Wolf, Y I, Koehorst, J J, Wurtzel, O, van der Oost, R, Ran, W, Blombach, F, Makarova, K S, Brouns, S J J, Forster, A C, Wagner, E G H, Sorek, R, Koonin, E V, van der Oost, J. Differential translation tunes uneven production of operon-encoded proteins. Cell Rep. 4, 938-944, 2013

Ieong, K-W, Pavlov, M Y, Kwiatkowski, M, Forster, A C, Ehrenberg, M. Inefficient delivery but fast peptide bond formation of unnatural L-aminoacyl-tRNAs in translation, J. Am. Chem. Soc. 134, 17955-17962, 2012

Punekar, A, Shepherd, T R, Liljeruhm, J, Forster, A C, Selmer, M. Crystal structure of RlmM, the 2'O-ribose methyltransferase for C2498 of E. coli 23S rRNA. Nucleic Acids Res., 40, 10507-10520, 2012

Forster, A C. Synthetic biology challenges long-held hypotheses in translation, codon bias and transcription. Biotech. J., 7, 835-845, 2012

Forster, A C, Lee, S Y. Editorial: NextGen SynBio has arrived... Biotech. J., 7, 827, 2012

Du, L, Villarreal, S, Forster, A C. Multigene expression in vivo: supremacy of large versus small terminators for T7 RNA polymerase. Biotechnol. Bioeng., 109, 1043-1050, 2012

Wang, H H, Huang, P-Y, Xu, G, Haas, W, Marblestone, A, Li, J, Gygi, S P, Forster, A C, Jewett, M C, Church, G M. Multiplexed in vivo His-tagging of enzyme pathways for in vitro single-pot multienzyme catalysis. ACS Synth. Biol., 1, 43-52, 2012

Watts, R E, Forster, A C. Update on pure translation display with unnatural amino acid incorporation. Meth. Mol. Biol., 805, 349-365, 2012

Gao, R, Forster, A C. Changeability of individual domains of an aminoacyl-tRNA in polymerization by the ribosome. FEBS Lett., 584(1), 99-105, 2010

Jewett, M C, Forster, A C. Update on designing and building minimal cells. Curr. Opin. Biotech., 21, 697-703, 2010

Watts, R E, Forster, A C. Chemical models of peptide formation in translation. Biochem., 49, 2177-2185, 2010

Du, L, Gao, R, Forster, A C. Engineering multigene expression in vitro and in vivo with small terminators for T7 RNA polymerase. Biotechnol. Bioeng., 104, 1189-1196, 2009

Forster, A C. Low modularity of aminoacyl-tRNA substrates in polymerization by the ribosome. Nucleic Acids Res., 37, 3747-3755, 2009

Pavlov, M Y, Watts, R E, Tan, Z, Cornish, V W, Ehrenberg, M, Forster, A C. Slow peptide bond formation by proline and other N-alkylamino acids in translation. Proc. Natl. Acad. Sci. USA, 106(1), 50-4, 2009

Forster, A C, Church, G M. Synthetic biology projects in vitro. Genome Res., 17(1), 1-6 and front cover, 2007

Zhang, B, Tan, Z, Gartenmann Dickson, L, Nalam, M N L, Cornish, V W, Forster, A C. Specificity of Translation for N-Alkyl Amino Acids. J. Am. Chem. Soc., 129(37), 11316-11317, 2007

Forster, A C, Church, G M. Towards synthesis of a minimal cell. Mol. Syst. Biol., 2(45), 1-10, 2006

Forster, A C. Engineering translation: A nano-review. Methods, 36(3), 225-6, 2005

Tan, Z, Blacklow, S C, Cornish, V W, Forster, A C. De novo genetic codes and pure translation display. Methods, 36(3), 279-90, 2005

Forster, A C, Cornish, V W, Blacklow, S C. Pure translation display. Anal. Biochem., 333(2), 358-64, 2004

Tan, Z, Forster, A C, Blacklow, S C, Cornish, V W. Amino acid backbone specificity of the Escherichia coli translation machinery. J. Am. Chem. Soc., 126(40), 12752-3, 2004

Forster, A C, Tan, Z, Nalam, M N L, Lin, H, Qu, H, Cornish, V W, Blacklow, S C. Programming peptidomimetic syntheses by translating genetic codes designed de novo. Proc. Natl. Acad. Sci. USA, 100(11), 6353-7, 2003

Forster, A C, Weissbach, H, Blacklow, S C. A simplified reconstitution of mRNA-directed peptide synthesis: activity of the epsilon enhancer and an unnatural amino acid. Anal. Biochem., 297(1), 60-70, 2001

Li, E, Beard, C, Forster, A C, Bestor, T H, Jaenisch, R. DNA methylation, genomic imprinting, and mammalian development. Cold Spring Harb. Symp. Quant. Biol., 58, 297-305, 1993

Forster, A C, Altman, S. External guide sequences for an RNA enzyme. Science, 249(4970), 783-6, 1990

Forster, A C, Altman, S. Similar cage-shaped structures for the RNA components of all ribonuclease P and ribonuclease MRP enzymes. Cell, 62(3), 407-9, 1990

Forster, A C, Davies, C, Hutchins, C J, Symons, R H. Characterization of self-cleavage of viroid and virusoid RNAs. Meth. Enzymol., 181, 583-607, 1990

McInnes, J L, Forster, A C, Skingle, D C, Symons, R H. Preparation and uses of photobiotin. Meth. Enzymol., 184, 588-600, 1990

Forster, A C, Davies, C, Sheldon, C C, Jeffries, A C, Symons, R H. Self-cleaving viroid and newt RNAs may only be active as dimers. Nature, 334(6179), 265-7, 1988

McInnes, J L, Forster, A C, Symons, R H. Photobiotin-labelled DNA and RNA hybridization probes. Meth. Mol. Biol., 4, 401-414, 1988

Forster, A C, Jeffries, A C, Sheldon, C C, Symons, R H. Structural and ionic requirements for self-cleavage of virusoid RNAs and trans self-cleavage of viroid RNA. Cold Spring Harb. Symp. Quant. Biol., 52, 249-59, 1987

Forster, A C, Symons, R H. Self-cleavage of virusoid RNA is performed by the proposed 55-nucleotide active site. Cell, 50(1), 9-16, 1987

Forster, A C, Symons, R H. Self-cleavage of plus and minus RNAs of a virusoid and a structural model for the active sites. Cell, 49(2), 211-20, 1987

Symons, R H, Hutchins, C J, Forster, A C, Rathjen, P D, Keese, P, Visvader, J E. Self-cleavage of RNA in the replication of viroids and virusoids. J. Cell Sci. Suppl., 7, 303-18, 1987

Hutchins, C J, Rathjen, P D, Forster, A C, Symons, R H. Self-cleavage of plus and minus RNA transcripts of avocado sunblotch viroid. Nucleic Acids Res., 14(9), 3627-40, 1986

Forster, A C, McInnes, J L, Skingle, D C, Symons, R H. Non-radioactive hybridization probes prepared by the chemical labelling of DNA and RNA with a novel reagent, photobiotin. Nucleic Acids Res., 13(3), 745-61, 1985

Visvader, J E, Forster, A C, Symons, R H. Infectivity and in vitro mutagenesis of monomeric cDNA clones of citrus exocortis viroid indicates the site of processing of viroid precursors. Nucleic Acids Res., 13(16), 5843-56, 1985

Lab pics