Abstract
There are three main groups of restriction endonucleases (REases) called Types I, II, and III (1,2). Since 1973, REases and DNA methyltransferases (MTases) have been named based on an original suggestion by Smith and Nathans (3). They proposed that the enzyme names should begin with a three-letter acronym in which the first letter was the first letter of the genus from which the enzyme was isolated and the next two letters were the first two letters of the species name. Extra letters or numbers could be added to indicate individual strains or serotypes. Thus, the enzyme Hindll was one of four enzymes isolated from H aemophilus in fluenzae serotype d.The first three letters of the name were italicized. Later, a formal proposition for naming the genes encoding REases and MTases was adopted (4). When there were only a handful of enzymes known, these schemes were very useful, but as more enzymes have been found, often from different genera and species with names whose three-letter acronyms would be identical, considerable laxity in naming conventions has appeared. In addition, we now know that each major type of enzyme can contain subtypes. This especially applies to the Type II enzymes, of which more than 3500 have been characterized (5). In this paper we revisit the naming conventions and outline an updated scheme that incorporates current knowledge about the complexities of these enzymes. We describe a set of naming conventions for REases and their associated MTases.
Originally published in Nucleic Acids Research, Vol. 31 No.7, 1805-1812 by Oxford University Press 2003. Reprinted with permission of Oxford University Press.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Boyer HW (1971) DNA restriction and modification mechanisms in bacteria. Annu Rev Microbiol 25:153–176
Yuan R (1981) Structure and mechanism of multifunctional restriction endonucleases. Annu Rev Biochem 50:285–315
Smith H O, Nathans D (1973) A suggested nomenclature for bacterial host modification and restriction systems and their enzymes. J Mol Biol 81:419–423
Szybalski W, Blumenthal RM, Brooks JE, Hattman S, Raleigh EA (1988) Nomenclature for bacterial genes coding for class-II restriction endonucleases and modification methyltransferases. Gene 74:279–280
Roberts RJ, Macelis D (2003) REBASE — restriction enzymes and methylases. Nucleic Acids Res 31:418–420
Belfort M, Roberts RJ (1997) Homing endonucleases: keeping the house in order. Nucleic Acids Res 25:3379–3388
Noyer-Weidner M, Jentsch S, Pawlek B, Gunthert U, Trautner TA (1983) Restriction and modification in Bacillus subtilis: DNA methylation potential of the related bacteriophages Z, SPR,SPb, f3T, and r11. J Virol 46:446–453
Klein R, Baranyi U, Rossler N, Greineder B, Scholz H, Witte A (2002) Natrialba magadii virus fCh1: first complete nucleotide sequence and functional organization of a virus infecting a haloalkaliphilic archaeon. Mol Microbiol 45:851–863
Karreman C, de Waard A (1990) Agmenellum quadruplicatum M.AquI, a novel modification methylase. J Bacteriol 172:266–272
Dryden DT, Murray NE, Rao DN (2001) Nucleoside triphosphate-dependent restriction enzymes. Nucleic Acids Res 29:3728–3741
Murray NE (2000) Type I restriction systems: sophisticated molecular machines. Microbiol Mol Biol Rev 64:412–434
Titheradge AJ, King J, Ryu J, Murray NE (2001) Families of restriction enzymes: an analysis prompted by molecular and genetic data for type ID restriction and modification systems. Nucleic Acids Res 29:4195–4205
Gubler M, Braguglia D, Meyer J, Piekarowicz A, Bickle TA (1992) Recombination of constant and variable modules alters DNA sequence recognition by type IC restriction-modification enzymes. EMBO J 11:233–240
Szybalski W, Kim SC, Hasan N, Podhajska AJ (1991) Class-IIS restriction enzymesa review. Gene 100:13–26
Stankevicius K, Lubys A, Timinskas A, Vaitkevicius D, Janulaitis A (1998) Cloning and analysis of the four genes coding for Bpul0I restriction-modification enzymes. Nucleic Acids Res 26:1084–1091
Looney MC, Moran LS, Jack WE, Feehery GR, Benner JS, Slatko BE, Wilson GG (1989) Nucleotide sequence of the FokI restriction-modification system: separate strandspecificity domains in the methyltransferase. Gene 80:193–208
Reuter M, Kupper D, Meisel A, Schroeder C, Kruger DH (1998) Cooperative binding properties of restriction endonuclease EcoRII with DNA recognition sites. J Biol Chern 273:8294–8300
Huai Q, Colandene JD, Topal MD, Ke H (2001) Structure of NaeI-DNA complex reveals dual-mode DNA recognition and complete dimer rearrangement. Nat Struct Biol 8:665–669
Xu Y, Lunnen KD, Kong H (2001) Engineering a nicking endonuclease N.AlwI by domain swapping. Proc Natl Acad Sci USA 98:12990–12995
Besnier CE, Kong H (2001) Converting MlyI endonuclease into a nicking enzyme by changing its oligomerization state. EMBO Rep 2:782–786
Hennecke F, Kolmar H, Brundl K, Fritz HJ (1991) The vsr gene product of E. coli K12 is a strand-and sequence-specific DNA mismatch endonuclease. Nature 253:776–778
Tao T, Bourne JC, Blumenthal RM (1991) A family of regulatory genes associated with Type II restriction-modification systems. J Bacteriol 173:1367–1375
Sohail A, Ives CL, Brooks JE (1995) Purification and characterization of C.BamHI, a regulator of the BamHI restrictionmodification system. Gene 157:227–228
Mucke M, Reich S, Moncke-Buchner E, Reuter M, Kruger DH (2001) DNA cleavage by type III restriction-modification enzyme EcoP15I is independent of spacer distance between two head to head oriented recognition sites. J Mol Biol 312:687–698
Ianscak P, Sandmeier U, Szczelkun MD, Bickle TA (2001) Subunit assembly and mode of DNA cleavage of the type III restriction endonucleases EcoP1I and EcoP15I. J Mol Biol 306:417–431
Raleigh EA, Wilson G (1986) Escherichia coli K-12 restricts DNA containing 5methylcytosine. Proc Natl Acad Sci USA 83:9070–9074
Stewart FJ, Panne D, Bickle TA, Raleigh EA (2000) Methylspecific DNA binding by McrBC, a modification-dependent restriction enzyme. J Mol Biol 298:611–622
Smith HO, Wilcox KW (1970) A restriction enzyme from Hemophilus influenzae. I. Purification and general properties. J Mol Biol 51:379–391
Kelly TJ Jr, Smith HO (1970) A restriction enzyme from Hemophilus influenzae. II. Base sequence of the recognition site. J Mol Biol 51:393–409
Roy PH, Smith HO (1973) DNA methylases of Hemophilus influenzae Rd. I. Purification and properties. J Mol Biol 81:427–444
Roy PH, Smith HO (1973) DNA methylases of Haemophilus influenzae Rd. II. Partial recognition site base sequences. J Mol Biol 81:445–459
Gromkova R, Bendler J, Goodgal S (1973) Restriction and modification of bacteriophage S2 in Haemophilus influenzae. J Bacteriol 114:1151–1157
Fleischmann RD, Adams MD, White O, Clayton RA, Kirkness EF, Kerlavage AR, Bult CJ, Tomb J, Dougherty BA, Merrick JM et al. (1995) Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269:496–512
Dusterhoft A, Erdmann D, and Kroger M (1991) Stepwise cloning and molecular characterization of the HgiDI restriction-modification system from Herpetosiphon giganteus Hpa2. Nucleic Acids Res 19:1049–1056
Belfort M, Derbyshire V, Cousineau B, Lambowitz A (2002) Mobile introns: pathways and proteins. In: Craig N, Craigie R, Gellert M, Lambowitz A (eds) Mobile DNA II. ASM Press, Washington, DC, pp 761–783
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2004 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Roberts, R.J. et al. (2004). A Nomenclature for Restriction Enzymes, DNA Methyltransferases, Homing Endonucleases, and Their Genes. In: Pingoud, A.M. (eds) Restriction Endonucleases. Nucleic Acids and Molecular Biology, vol 14. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-18851-0_1
Download citation
DOI: https://doi.org/10.1007/978-3-642-18851-0_1
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-62324-0
Online ISBN: 978-3-642-18851-0
eBook Packages: Springer Book Archive