Publications
- AG Sträßer
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Kern, C., Radon, C., Wende, W., Leitner, A. and Sträßer, K. (2023) Cross-linking mass spectrometric analysis of the endogenous TREX complex from S. cerevisiae. RNA
Keil, P., Wulf, A., Kachariya, N., Reuscher, S., Hühn, K., Silbern, I., Altmüller, J., Keller, M., Stehle, R., Zarnack, K., Sattler, M., Urlaub, H. and Sträßer, K. (2022) Npl3 functions in mRNP assembly by recruitment of mRNP components to the transcription site and their transfer onto the mRNA. Nucleic Acids Res. 51:831-851
Zarnack, K., Balasubramanian, S., Gantier, M.P., Kunetsky, V., Kracht, M., Schmitz, M.L. and Sträßer, K. (2020) Dynamic mRNP remodeling in response to internal and external stimuli. Biomolecules 2020, 10:1310
Wende, W., Friedhoff, P., Sträßer, K. (2019) Mechanism and Regulation of Co-transcriptional mRNP Assembly and Nuclear mRNA Export. In: Oeffinger M., Zenklusen D. (eds) The Biology of mRNA: Structure and Function. Advances in Experimental Medicine and Biology, vol 1203. Springer, Cham.Minocha, R., Popova, V., Kopytova, D., Misiak, D., Hüttelmaier, S., Georgieva, S. and Sträßer, K. (2018) Mud2 functions in transcription by recruiting the Prp19 and TREX complexes to transcribed genes. Nucleic Acids Res. 46:9749-9763
Reuter, L.M. and Sträßer, K. (2016) Falling for the dark side of transcription: Nab2 fosters RNA polymerase III transcription. Transcription 7: 69-74
Reuter, L.M., Meinel, D.M., and Sträßer, K. (2015) The poly(A)-binding protein Nab2 functions in RNA polymerase III transcription. Genes Dev. 29: 1565-1575
Meinel, D.M. and Sträßer, K. (2015) Co-transcriptional mRNP formation is coordinated within a molecular mRNP packaging station in S. cerevisiae. Bioessays 37: 666-677
Coordes, B., Brünger, K.M., Burger, K., Soufi, B., Horenk, J., Eick, D., Olsen, J.V., and Sträßer, K. (2015) Ctk1 function is necessary for full translation initiation activity in Saccharomyces cerevisiae. Eukaryot Cell 14: 86-95
Karakasili, E.*, Burkert-Kautzsch, C.*, Kieser, A., and Sträßer, K. (2014) Degradation of DNA damage-independently stalled RNA polymerase II is independent of the E3 ligase Elc1. Nucleic Acids Res. 42: 10503-10515
* equal contribution
Meinel, D.M., Burkert-Kautzsch, C., Kieser, A., O’Duibhir, E., Siebert, M., Mayer, A., Cramer, P., Söding, J., Holstege, F.C., and Sträßer, K. (2013) Recruitment of TREX to the Transcription Machinery by its Direct Binding to the Phospho-CTD of RNA Polymerase II. PLoS Genetics 9: e1003914
Burger, K., Mühl, B., Rohrmoser M., Coordes, B., Heidemann, M., Kellner, M., Gruber-Eber, A., Heissmeyer, V., Sträßer, K., and Eick, D. (2013) Cyclin-dependent kinase 9 links RNA Polymerase II transcription to processing of ribosomal RNA. J. Biol. Chem. 288: 21173-21183
Chanarat, S. and Sträßer, K. (2013) Splicing and beyond: The many faces of the Prp19 complex. BBA-MCR 1833: 2126-2134 (review)
Miller, C., Matic, I., Maier, K., Schwalb, B., Röther, S., Sträßer, K., Tresch, A., Mann, M., and Cramer, P. (2012) Mediator phosphorylation prevents stress response transcription during non-stress conditions. J. Biol. Chem. 287: 44017-44026
Schiller, C., Lammens, K., Guerini, I., Coordes, B., Schlauderer, F., Möckel, C., Schele, A., Sträßer, K., Jackson, S.P., and Hopfner, K.-P. (2012) Structure of Mre11-Nbs1 complex yields insights into ataxia-telangiectasia-like disease mutations and DNA damage signaling. Nat. Struct. Mol. Biol. 19: 693-700
Chanarat, S., Burkert-Kautzsch, C., Meinel, D.M., and Sträßer, K. (2012) Prp19C and TREX: Interacting to promote transcription elongation and mRNA export. Transcription 3: 8-12 (review)
Schenk, L., Meinel D.M., Sträßer, K., and Gerber A.P. (2012) La-motif dependent mRNA binding of La-related proteins mediates copper detoxification in yeast. RNA 18: 449-461
Chanarat, S., Seizl, M., and Sträßer, K. (2011) The Prp19 Complex is a Novel Transcription Elongation Factor Required for TREX Occupancy at Transcribed Genes. Genes Dev. 25: 1147-1158
Lammens, K.*, Bemeleit, D.J.*, Möckel, C.*, Clausing, E., Schele, A., Hartung, S., Schiller, C.B., Lucas, M., Angermüller, C., Söding, J., Sträßer, K., and Hopfner, K.-P. (2011) The Mre11:Rad50 complex shows an ATP-dependent molecular clamp in DNA double-strand break repair. Cell 145: 54-66
* equal contribution
Clausing, E., Mayer, A.*, Chanarat, S.*, Müller, B., Germann, S.M., Cramer, P., Lisby, M., and Sträßer, K. (2010) The transcription elongation factor Bur1-Bur2 interacts with Replication Protein A to maintain genome stability. J. Biol. Chem. 285: 41665-41674
* equal contribution
Röther, S.*, Burkert, C.*, Brünger, K.M.*, Mayer, A.*, Kieser, A., and Sträßer, K. (2010) Nucleocytoplasmic shuttling of the La motif-containing protein Sro9 might link its nuclear and cytoplasmic functions. RNA 16: 1393-1401
* equal contribution
Röther, S. and Sträßer, K. (2009) mRNA Export – an integrative component of gene expression. In: Nuclear Transport, edited by Ralph Kehlenbach, Austin: Landes Bioscience, review
Jasiak, A.J., Hartmann, H., Karakasili, E., Marian, K., Flatley, A., Kremmer, E., Sträßer, K., Martin, D.E., Söding, J., and Cramer, P. (2008) Genome-associated RNA polymerase II includes the dissociable RPB4/7 subcomplex. J. Biol. Chem. 283: 26423-7
Larivière, L., Seizl, M., van Wageningen, S., Roether, S., Feldmann, H., Sträßer, K., Hahn, S., Holstege, F., and Cramer, P. (2008) Structure-system correlation identifies a gene regulatory Mediator submodule. Genes Dev. 22: 872-877
Röther, S. and Sträßer, K. (2007) The RNA polymerase II CTD kinase Ctk1 functions in translation elongation. Gen. Dev. 21: 1409-1421
Covered by the perspective “Synchronicity: policing multiple aspects of gene expression by Ctk1” by M. Hampsey and T. G. Kinzy in the same issue of Gen. Dev.
Krebs, S., Medugorac, I., Röther, S., Sträßer, K., and Förster, M. (2007) A missense mutation in the 3-ketodihydrosphingosine reductase FVT1 as candidate causal mutation for bovine spinal muscular atrophy. Proc. Natl. Ac. Sc. USA 104: 6746-51
Röther, S., Clausing, E., Kieser, A., and Sträßer, K. (2006) Swt1, a novel yeast protein, functions in transcription. J. Biol. Chem. 281: 36518 - 36525
Larivière, L., Geiger, S., Hoeppner, S., Röther, S., Sträßer, K., and Cramer, P. (2006) Structure and TBP binding of the Mediator head subcomplex Med8–Med18–Med20. Nat. Struct. Mol. Biol. 13: 895 - 901
Cramer, P., Sträßer, K., Niessing, D., Meister, G., and Jansen, R.P. (2005) RNA als Koordinator und Regulator der Genexpression. BIOspektrum, Sonderausgabe, 11. Jahrgang, 523-525
Hurt, E., Luo, M.J., Röther, S., Reed, R., and Sträßer, K. (2004) Cotranscriptional recruitment of the serine-arginine-rich (SR)-like proteins Gbp2 and Hrb1 to nascent mRNA via the TREX complex. Proc. Natl. Ac. Sc. USA 101: 1858-1862
Fischer, T., Sträßer, K., Rácz, A., Rodriguez-Navarro, S., Oppizzi, M., Ihrig, P., Lechner, J., and Hurt, E. (2002) The mRNA export machinery requires the novel Sac3-Thp1 complex to dock at the nucleoplasmic entrance of the nuclear pores. EMBO J. 21: 5843-5852
Sträßer, K. (2002) Nukleärer mRNA-Export: Wie die messenger RNA vom Genlocus zu den Kernporen gelangt. BIOspektrum 5/02: 636/7
Sträßer, K. , Masuda, S., Mason, P., Pfannstiel J., Oppizzi M., Rodriguez-Navarro S., Rondón A.G., Aguilera A., Struhl, K., Reed R., and Hurt E. (2002) TREX is a conserved complex coupling transcription with messenger RNA export. Nature 417: 304-308
Rodríguez-Navarro, S., Sträßer, K., and Hurt, E. (2002) An intron in the YRA1 gene is required to control Yra1p protein expression and mRNA export in yeast. EMBO R. 3: 438-442
Katahira, J., Sträßer, K., Saiwaki, T., Yoneda, Y., and Hurt, E. (2002) Complex formation between Tap and p15 affects binding to FG-repeat nucleoporins and nucleocytoplasmic shuttling. J. Biol. Chem. 277: 9242-9246
Sträßer, K. and Hurt, E. (2001) Splicing factor Sub2p is required for nuclear mRNA export through its interaction with Yra1p. Nature 413:648-652
Zhou, Z., Luo, M., Sträßer, K., Katahira, J., Hurt, E., and Reed, R. (2000) The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans. Nature 407: 401-405
Sträßer, K., Baßler, J., and Hurt, E. (2000) Binding of the Mex67p/Mtr2p Heterodimer to FXFG-, GLFG-, and FG-Repeat Nucleoporins is essential for Nuclear mRNA Export. J. Cell Biol. 150:695-706
Hurt, E., Sträßer, K., Segref, A., Bailer, S., Schlaich, N., Presutti, C., Tollervey, D., and Jansen, R. (2000) Mex67p mediates nuclear export of a variety of RNA polymerase II transcripts. J. Biol. Chem. 275: 8361-8368
Sträßer, K. and Hurt, E. (2000) Yra1p, a conserved nuclear RNA-binding protein, interacts directly with Mex67p and is required for mRNA export. EMBO J. 19: 410-420
Sträßer, K. and Hurt, E. (1999) Nuclear RNA export in yeast (review). FEBS Letters 452: 77-81
Katahira, J., Sträßer, K., Podtelejnikov, A., Mann, M., Jung, J.U., and Hurt, E. (1999) The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to human. EMBO J. 18: 2593-2609
Vassella, E., Sträßer, K., and Boshart, M. (1997) A mitochondrion-specific dye for multicolour fluorescent imaging of Trypanosoma brucei. Mol. Biochem. Parasitol. 90: 381-385
- AG Friedhoff
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Monakhova, M., Ryazanova, A., Kunetsky, V., Li, P., Shilkin, E., Kisil, O., Rao, D.N., Oretskaya, T., Friedhoff, P. and Kubareva, E. (2020) Probing the DNA-binding center of the MutL protein from the Escherichia coli mismatch repair system via crosslinking and Förster resonance energy transfer. Biochimie, 171-172: 43-54.
Wende, W., Friedhoff, P., Sträßer, K. (2019) Mechanism and Regulation of Co-transcriptional mRNP Assembly and Nuclear mRNA Export. In: Oeffinger M., Zenklusen D. (eds) The Biology of mRNA: Structure and Function. Advances in Experimental Medicine and Biology, vol 1203. Springer, Cham.
Schneider, T., Hung, L.H., Aziz, M., Wilmen, A., Thaum, S., Wagner, J., Janowski, R., Müller, S., Schreiner, S., Friedhoff, P., Hüttelmaier, S., Niessing, D., Sattler, M., Schlundt, A. and Bindereif, A. (2019) Combinatorial recognition of clustered RNA elements by the multidomain RNA-binding protein IMP3. Nature communications, 10:2266.
Mardenborough, Y.S.N., Nitsenko, K., Laffeber, C., Duboc, C., Sahin, E., Quessada-Vial, A., Winterwerp, H.H.K., Sixma, T.K., Kanaar, R., Friedhoff, P., Strick, T.R. and Lebbink, J.H.G. (2019) The unstructured linker arms of MutL enable GATC site incision beyond roadblocks during initiation of DNA mismatch repair. Nucleic acids research, 47:11667-11680.
Monakhova, M.V., Penkina, A.I., Pavlova, A.V., Lyaschuk, A.M., Kucherenko, V.V., Alexeevski, A.V., Lunin, V.G., Friedhoff, P., Klug, G., Oretskaya, T.S. and Kubareva, E.A. (2018) Endonuclease Activity of MutL Protein of the Rhodobacter sphaeroides Mismatch Repair System. Biochemistry. Biokhimiia, 83: 281-29.
Friedhoff, P., Manelyte, L., Giron-Monzon, L., Winkler, I., Groothuizen, F.S. and Sixma, T.K. (2017) Use of Single-Cysteine Variants for Trapping Transient States in DNA Mismatch Repair. Methods in enzymology, 592:77-101.
Hermans N, Laffeber C, Cristovão M, Artola-Borán M, Mardenborough Y, Ikpa P, Jaddoe A, Winterwerp HH, Wyman C, Jiricny J, Kanaar R, Friedhoff P and Lebbink JH. (2016) Dual daughter strand incision is processive and increases the efficiency of DNA mismatch repair. Nucleic Acids Res. 44(14):6770-86.
Friedhoff P, Li P, and Gotthardt J. (2016) Protein-protein interactions in DNA mismatch repair. DNA Repair 38: 50-7.
Groothuizen FS, Winkler I, Cristóvão M, Fish A, Winterwerp HH, Reumer A, Marx AD, Hermans N, Nicholls RA, Murshudov GN, Lebbink JH, Friedhoff P and Sixma TK. (2015) MutS/MutL crystal structure reveals that the MutS sliding clamp loads MutL onto DNA. Elife 4: e06744.
Perevozchikova SA, Trikin RM, Heinze RJ, Romanova EA, Oretskaya TS, Friedhoff P, Kubareva EA. (2014) Is thymidine glycol containing DNA a substrate of E. coli DNA mismatch repair system? PLoS One. Aug 18;9(8):e104963.
Perevoztchikova SA, Romanova EA, Oretskaya TS, Friedhoff P, Kubareva EA. (2013) Modern aspects of the structural and functional organization of the DNA mismatch repair system. Acta Naturae Jul;5(3):17-34.
Groothuizen FS, Fish A, Petoukhov MV, Reumer A, Manelyte L, Winterwerp HH, Marinus MG, Lebbink JH, Svergun DI, Friedhoff P, Sixma TK. (2013) Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation. Nucleic Acids Res. Sep;41(17):8166-81.
Gabsalilow L, Schierling B, Friedhoff P, Pingoud A, Wende W. (2013) Site- and strand-specific nicking of DNA by fusion proteins derived from MutH and I-SceI or TALE repeats. Nucleic Acids Res. Apr;41(7):e83.
Heinze RJ, Sekerina S, Winkler I, Biertümpfel C, Oretskaya TS, Kubareva E, Friedhoff P. (2012) Covalently trapping MutS on DNA to study DNA mismatch recognition and signaling. Mol Biosyst. Jul 6;8(7):1861-4.
Cristóvão M, Sisamakis E, Hingorani MM, Marx AD, Jung CP, Rothwell PJ, Seidel CA, Friedhoff P. (2012) Single-molecule multiparameter fluorescence spectroscopy reveals directional MutS binding to mismatched bases in DNA. Nucleic Acids Res. Jul 1;40(12):5448-5464.
Midon M, Gimadutdinow O, Meiss G, Friedhoff P, Pingoud A. (2012) Chemical rescue of active site mutants of the S. pneumoniae surface endonuclease EndA and other nucleases of the H-N-H family by imidazole. ChemBioChem 13, 713-721.
Xiao Y, Jung C, Marx AD, Winkler I, Wyman C, Lebbink JH, Friedhoff P, Cristovao M. (2011) Generation of DNA nanocircles containing mismatched bases. Biotechniques Oct;51(4):259-62, 264-5.
Ryazanova AY, Winkler I, Friedhoff P, Viryasov MB, Oretskaya TS, Kubareva EA. (2011) Crosslinking of (cytosine-5)-DNA methyltransferase SsoII and its complexes with specific DNA duplexes provides an insight into their structures. Nucleosides Nucleotides Nucleic Acids Jul-Aug;30(7-8):632-50.
Monti MC, Cohen SX, Fish A, Winterwerp HH, Barendregt A, Friedhoff P, Perrakis A, Heck AJ, Sixma TK, van den Heuvel RH, Lebbink JH. (2011) Native mass spectrometry provides direct evidence for DNA mismatch-induced regulation of asymmetric nucleotide binding in mismatch repair protein MutS. Nucleic Acids Res. Oct;39(18):8052-64.
Winkler I, Marx AD, Lariviere D, Heinze R, Cristovao M, Reumer A, Curth U, Sixma TK, Friedhoff P. (2011) Chemical trapping of the dynamic MUTS-MUTL complex formed in DNA mismatch repair in Escherichia coli. J Biol Chem. May 13;286(19):17326-37.
Hanstein S, Wang X, Qian X, Friedhoff P, Fatima A, Shan Y, Feng K, Schubert S. (2011) Changes in cytosolic Mg2+ levels can regulate the activity of the plasma membrane H+-ATPase in maize. Biochem J. Apr 1;435(1):93-101.
Riazanova AIu, Molochkov NV, Abrosimova LA, Alekseevskiĭ AV, Kariagina AS, Protsenko AS, Friedhoff P, Oretskaia TS, Kubareva EA. (2010) Secondary structure of SsoII-like (cytosine-5)-DNA methyltransferases N-terminal region determined by circular dichroism spectroscopy. Mol Biol (Mosk) Sep-Oct;44(5):911-21. Russian.
Namadurai S, Jain D, Kulkarni DS, Tabib CR, Friedhoff P, Rao DN, Nair DT. (2010) The C-terminal domain of the MutL homolog from Neisseria gonorrhoeae forms an inverted homodimer. PLoS One Oct 28;5(10):e13726.
- AG Wende
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Mankai, H., Wende, W., Slama, N., Ayed, A., Roberts, R.J., Limam, F. (2020) Biochemical and molecular characterization of a restriction endonuclease Tvu2HI from Thermoactinomyces vulgaris 2H and study of its R-M system. International Journal of Biological Macromolecules, 164:3105-3113.
Wende, W., Friedhoff, P., Sträßer, K. (2019) Mechanism and Regulation of Co-transcriptional mRNP Assembly and Nuclear mRNA Export. In: Oeffinger M., Zenklusen D. (eds) The Biology of mRNA: Structure and Function. Advances in Experimental Medicine and Biology, vol 1203. Springer, Cham.
Yanik M, Ponnam SPG, Wimmer T, Trimborn L, Müller C, Gambert I, Ginsberg J, Janise A, Domicke J, Wende W, Lorenz B, Stieger K. (2018)
Development of a reporter system to explore MMEJ in the context of replacing large genomic fragments.
Mol. Ther. Nucleic Acids. 11:407-415.Yanik M, Wende W, Stieger K. (2017) Genome editing tools and their application in
experimental ophthalmology. Klin. Monbl. Augenheilkd. 234(3):329-334.Yanik M, Müller B, Song F, Gall J, Wagner F, Wende W, Lorenz B, Stieger K. (2017)
In vivo genome editing as a potential treatment strategy for inherited retinal
dystrophies. Prog. Retin. Eye Res. 56:1-18.Abrosimova LA, Kubareva EA, Migur AY, Gavshina AV, Ryazanova AY, Norkin MV, Perevyazova TA, Wende W, Hianik T, Zheleznaya LA and Oretskaya TS. (2016) Peculiarities of the interaction of the restriction endonuclease BspD6I with DNA containing its recognition site. Biochim Biophys Acta. 1864(9):1072-1082.
Ruiz-Heiland G, Jabir S, Wende W, Blecher S, Bock N and Ruf S. (2016) Novel missense mutation in the EDA gene in a family affected by oligodontia. J. Orofac. Orthop. 77(1):31-8.
Pingoud A, Wilson GG, Wende W. (2014) Type II restriction endonucleases - a historical perspective and more. Nucleic Acids Res.;42(12):7489-527.
Zuravka I, Roesmann R, Sosic A, Wende W, Pingoud A, Gatto B, Göttlich R. (2014) Synthesis and DNA cleavage activity of Bis-3-chloropiperidines as alkylating agents. ChemMedChem 9(9):2178-85.
Yanik M, Alzubi J, Lahaye T, Cathomen T, Pingoud A, Wende W. (2013) TALE-PvuII Fusion Proteins - Novel Tools for Gene Targeting. PLoS ONE 8(12): e82539.
Abrosimova LA, Monakhova MV, Migur AYu, Wende W, Pingoud A, Kubareva EA, Oretskaya TS. (2013) Thermo-switchable activity of the restriction endonuclease SsoII achieved by site-directed enzyme modification. IUBMB Life 65(12):1012-1016.
Heller I, Sitters G, Broekmans OD, Farge G, Menges C, Wende W, Hell SW, Peterman EJ, Wuite GJ. (2013) STED nanoscopy combined with optical tweezers reveals protein dynamics on densely covered DNA. Nature Methods 10(9):910-916.
Gabsalilow L, Schierling B, Friedhoff P, Pingoud A, Wende W. (2013) Site- and strand-specific nicking of DNA by fusion proteins derived from MutH and I-SceI or TALE repeats. Nucleic Acids Res. Apr;41(7):e83.
Otero JM, Noël AJ, Guardado-Calvo P, Llamas-Saiz AL, Wende W, Schierling B, Pingoud A, van Raaij MJ. (2012) High-resolution structures of Thermus thermophilus enoyl-acyl carrier protein reductase in the apo form, in complex with NAD+ and in complex with NAD+ and triclosan. Acta Crystallogr Sect F Struct Biol Cryst Commun. 68(Pt 10):1139-48.
Schierling B, Wende W, Pingoud A. (2012) Redesigning the single-chain variant of the restriction endonuclease PvuII by circular permutation. FEBS Lett. 586(12):1736-41.
Dikic J, Menges C, Clarke S, Kokkinidis M, Pingoud A, Wende W, Desbiolles P. (2012) The rotation-coupled sliding of EcoRV. Nucleic Acids Res. May;40(9):4064-70.
Schierling B, Dannemann N, Gabsalilow L, Wende W, Cathomen T, Pingoud A. (2012) A novel zinc-finger nuclease platform with a sequence-specific cleavage module. Nucleic Acids Res. Mar;40(6):2623-38.
Fonfara I, Curth U, Pingoud A, Wende W. (2012) Creating highly specific nucleases by fusion of active restriction endonucleases and catalytically inactive homing endonucleases. Nucleic Acids Res Jan;40(2):847-60.
Hien le T, Zatsepin TS, Schierling B, Volkov EM, Wende W, Pingoud A, Kubareva EA, Oretskaya TS. (2011) Restriction endonuclease SsoII with photoregulated activity - a "molecular gate" approach. Bioconjug Chem. Jul 20;22(7):1366-73.
Pingoud A, Wende W. (2011) Generation of novel nucleases with extended specificity by rational and combinatorial strategies. Chembiochem Jul 4;12(10):1495-500.
Silanskas A, Foss M, Wende W, Urbanke C, Lagunavicius A, Pingoud A, Siksnys V. (2011) Photocaged Variants of the MunI and PvuII Restriction Enzymes. Biochemistry Apr 12;50(14):2800-7.
Grishin A, Fonfara I, Alexeevski A, Spirin S, Zanegina O, Karyagina A, Alexeyevsky D, Wende W. (2010) Identification of conserved features of LAGLIDADG homing endonucleases. J Bioinform Comput Biol. Jun;8(3):453-69.
Schierling B, Noël AJ, Wende W, Hien le T, Volkov E, Kubareva E, Oretskaya T, Kokkinidis M, Römpp A, Spengler B, Pingoud A. (2010) Controlling the enzymatic activity of a restriction enzyme by light. Proc Natl Acad Sci USA. Jan 26;107(4):1361-6.