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1.
Dokl Biochem Biophys ; 512(1): 245-250, 2023 Oct.
Artigo em Inglês | MEDLINE | ID: mdl-38093124

RESUMO

DNA polymerase λ (Polλ) belongs to the same structural X-family as DNA polymerase ß, the main polymerase of base excision repair. The role of Polλ in this process remains not fully understood. A significant difference between the two DNA polymerases is the presence of an extended non-catalytic N-terminal region in the Polλ structure. The influence of this region on the interaction of Polλ with DNA and multifunctional proteins, poly(ADP-ribose)polymerase 1 (PARP1) and replication protein A (RPA), was studied in detail for the first time. The data obtained suggest that non-catalytic Polλ domains play a suppressor role both in relation to the polymerase activity of the enzyme and in interaction with DNA and PARP1.


Assuntos
DNA Polimerase beta , Reparo do DNA , DNA Polimerase beta/metabolismo , DNA
2.
Mol Biol (Mosk) ; 55(2): 181-193, 2021.
Artigo em Russo | MEDLINE | ID: mdl-33871434

RESUMO

The base and nucleotide excision DNA repair (BER and NER) systems are aimed at removing specific types of damaged DNA, i.e., oxidized, alkylated, or deaminated bases in the case of BER and bulky damage caused by UV radiation or chemical carcinogens in the case of NER. In some cases, however, the repair process follows a more complex scenario, which implies that the repair pathways exchange proteins and interact with each other to form a common interactome. This review describes the BER and NER mechanisms and discusses the current data on the involvement of the NER proteins in the repair of DNA lesions caused by oxidative stress and the BER proteins in the removal of bulky DNA adducts. We also discuss the role of poly(ADP-ribose) polymerase 1 in the regulation of the BER and NER processes and their coordination in the repair of complex (cluster) lesions.


Assuntos
Dano ao DNA , Reparo do DNA , DNA/genética , DNA/metabolismo , Reparo do DNA/genética , Nucleotídeos , Estresse Oxidativo/genética
3.
Biochemistry (Mosc) ; 84(9): 1008-1020, 2019 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-31693460

RESUMO

Nucleotide excision repair (NER) is one of the major DNA repair pathways aimed at maintaining genome stability. Correction of DNA damage by the NER system is a multistage process that proceeds with the formation of multiple DNA-protein and protein-protein intermediate complexes and requires precise coordination and regulation. NER proteins undergo post-translational modifications, such as ubiquitination, sumoylation, phosphorylation, acetylation, and poly(ADP-ribosyl)ation. These modifications affect the interaction of NER factors with DNA and other proteins and thus regulate either their recruitment into the complexes or dissociation from these complexes at certain stages of DNA repair, as well as modulate the functional activity of NER proteins and control the process of DNA repair in general. Here, we review the data on the post-translational modifications of NER factors and their effects on DNA repair. Protein poly(ADP-ribosyl)ation catalyzed by poly(ADP-ribose) polymerase 1 and its impact on NER are discussed in detail, since such analysis has not been done before.


Assuntos
Reparo do DNA , Proteínas de Ligação a DNA/química , Proteínas de Ligação a DNA/metabolismo , Nucleotídeos/metabolismo , Processamento de Proteína Pós-Traducional , Humanos
4.
Biochemistry (Mosc) ; 81(3): 233-41, 2016 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-27262192

RESUMO

The combined action of reactive metabolites of benzo[a]pyrene (B[a]P) and oxidative stress can lead to cluster-type DNA damage that includes both a bulky lesion and an apurinic/apyrimidinic (AP) site, which are repaired by the nucleotide and base excision repair mechanisms - NER and BER, respectively. Interaction of NER protein XPC-RAD23B providing primary damage recognition with DNA duplexes containing a B[a]P-derived residue linked to the exocyclic amino group of a guanine (BPDE-N(2)-dG) in the central position of one strand and AP site in different positions of the other strand was analyzed. It was found that XPC-RAD23B crosslinks to DNA containing (+)-trans-BPDE-N(2)-dG more effectively than to DNA containing cis-isomer, independently of the AP site position in the opposite strand; protein affinity to DNA containing one of the BPDE-N(2)-dG isomers depends on the AP site position in the opposite strand. The influence of XPC-RAD23B on hydrolysis of an AP site clustered with BPDE-N(2)-dG catalyzed by the apurinic/apyrimidinic endonuclease 1 (APE1) was examined. XPC-RAD23B was shown to stimulate the endonuclease and inhibit the 3'-5' exonuclease activity of APE1. These data demonstrate the possibility of cooperation of two proteins belonging to different DNA repair systems in the repair of cluster-type DNA damage.


Assuntos
Benzo(a)pireno/metabolismo , Adutos de DNA/metabolismo , Reparo do DNA , DNA/metabolismo , Marcadores de Afinidade , Sequência de Bases , Benzo(a)pireno/química , DNA/química , Adutos de DNA/química , Dano ao DNA , Enzimas Reparadoras do DNA/genética , Enzimas Reparadoras do DNA/metabolismo , DNA Liase (Sítios Apurínicos ou Apirimidínicos)/genética , DNA Liase (Sítios Apurínicos ou Apirimidínicos)/metabolismo , Proteínas de Ligação a DNA/genética , Proteínas de Ligação a DNA/metabolismo , Humanos , Ligação Proteica , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/química , Proteínas Recombinantes/isolamento & purificação
5.
Mol Biol (Mosk) ; 50(5): 735-750, 2016.
Artigo em Russo | MEDLINE | ID: mdl-27830676

RESUMO

Replication protein A (RPA) is a key regulator of eukaryotic DNA metabolism. RPA is a highly conserved heterotrimeric protein and contains multiple oligonucleotide/oligosaccharide-binding folds. The major RPA function is binding to single-stranded DNA (ssDNA) intermediates forming in DNA replication, repair, and recombination. Although binding ssDNA with high affinity, RPA can rapidly diffuse along ssDNA and destabilizes the DNA secondary structure. A highly dynamic RPA binding to ssDNA allows other proteins to access ssDNA and to displace RPA from the RPA-ssDNA complex. As has been shown recently, RPA in complex with ssDNA is posttranslationally modified in response to DNA damage. These modifications modulate the RPA interactions with its protein partners and control the DNA damage signaling pathways. The review considers up-to-date data on the RPA function as an active coordinator of ssDNA intermediate processing within DNA metabolic pathways, DNA repair in particular.


Assuntos
Reparo do DNA/fisiologia , Replicação do DNA/fisiologia , DNA de Cadeia Simples/metabolismo , Células Eucarióticas/metabolismo , Proteína de Replicação A/metabolismo , Animais , DNA de Cadeia Simples/genética , Humanos , Proteína de Replicação A/genética
6.
Bioorg Khim ; 41(5): 531-8, 2015.
Artigo em Russo | MEDLINE | ID: mdl-26762090

RESUMO

Genomic DNA is constantly damaged by the action of exogenous factors and endogenous reactive metabolites. Apurinic/apyrimidinic sites (AP sites), which occur as a result of DNA glycosylase induced or spontaneous hydrolysis of the N-glycosidic bonds, are the most common damages of DNA. The chemical reactivity of AP sites is the cause of DNA breaks, and DNA-protein and DNA-DNA crosslinks. Repair of AP sites is one of the most important mechanisms for maintaining genome stability. Despite the fact that the main participants of the AP site repair are very well studied, the new proteins that could be involved potentially in this process as "back up" players or perform certain specialized functions are being found. This review is dedicated to one of these proteins, tyrosyl-DNA phosphodiesterase 1 (Tdp1), for which we have recently shown that in addition to its main activity of specific cleavage of the tyrosyl-DNA bond formed via a covalent attachment of topoisomerase 1 (Top1) to DNA, Tdp1 is able to initiate the cleavage of the internal AP sites in DNA and their following repair. Tdp1 was discovered in Saccharomyces cerevisiae yeast as an enzyme hydrolyzing the covalent bond between tyrosyl residue of topoisomerase 1 and 3'-phosphate group in DNA. Tdp1 is the major enzyme which carries out the repair of the irreversible complexes of DNA and topoisomerase 1, which appear. in the presence of Top 1 inhibitors, such as camptothecin, therefore Tdp1 is a very important target for the development of inhibitors--anticancer drugs. Besides, Tdp1 hydrolyzes a wide range of 3'-terminal DNA modifications and the 3'-end nucleosides and its derivatives to form a 3'-phosphate. Tdp1 ability to cleave AP sites suggests its involvement in the base excision repair as an alternative enzyme to cleave AP sites instead of AP endonuclease 1--the major enzyme hydrolyzing AP sites in DNA repair process.


Assuntos
Ácido Apurínico/química , Dano ao DNA , Reparo do DNA/genética , Conformação de Ácido Nucleico , Diester Fosfórico Hidrolases/química , Polinucleotídeos/química , Animais , Sítios de Ligação , DNA/química , Humanos , Hidrólise
7.
Biochemistry (Mosc) ; 79(6): 545-54, 2014 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-25100013

RESUMO

Xeroderma pigmentosum factor A (XPA) is one of the key proteins in the nucleotide excision repair (NER) process. The effects of point substitutions in the DNA-binding domain of XPA (positively charged lysine residues replaced by negatively charged glutamate residues: XPA K204E, K179E, K141E, and tandem mutant K141E/K179E) on the interaction of the protein with DNA structures modeling intermediates of the damage recognition and pre-incision stages in NER were analyzed. All these mutations decreased the affinity of the protein to DNA, the effect depending on the substitution and the DNA structure. The mutant as well as wild-type proteins bind with highest efficiency partly open damaged DNA duplex, and the affinity of the mutants to this DNA is reduced in the order: K204E > K179E >> K141E = K141/179E. For all the mutants, decrease in DNA binding efficiency was more pronounced in the case of full duplex and single-stranded DNA than with bubble-DNA structure, the difference between protein affinities to different DNA structures increasing as DNA binding activity of the mutant decreased. No effect of the studied XPA mutations on the location of the protein on the partially open DNA duplex was observed using photoinduced crosslinking with 5-I-dUMP in different positions of the damaged DNA strand. These results combined with earlier published data suggest no direct correlation between DNA binding and activity in NER for these XPA mutants.


Assuntos
Reparo do DNA , DNA/metabolismo , Proteína de Xeroderma Pigmentoso Grupo A/metabolismo , Substituição de Aminoácidos , Sequência de Bases , DNA/química , Dano ao DNA , Escherichia coli/metabolismo , Humanos , Conformação de Ácido Nucleico , Ligação Proteica , Estrutura Terciária de Proteína , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteína de Xeroderma Pigmentoso Grupo A/química , Proteína de Xeroderma Pigmentoso Grupo A/genética
8.
Mol Biol (Mosk) ; 47(5): 731-42, 2013.
Artigo em Russo | MEDLINE | ID: mdl-25509345

RESUMO

The genomic DNA is damaged under the influence of different environmental factors such as air pollutions, ultraviolet and ionizing radiation, and toxic substances that negatively impact on the humans. Air pollution by the products of incomplete combustion of hydrocarbon fuels and waste of various industries are main sources of polycyclic aromatic hydrocarbons. Some metabolites of these compounds can damage DNA through forming the bulky DNA adducts that potentially leads to mutagenesis and cancer. A nucleotide excision repair is the major pathway for the reparation of such DNA lesions in eukaryotic cells. The excision efficiency of bulky adducts depends on many factors including the structure of a substituent and degree of DNA double helix distortion induced by a lesion. The most danger for cell is clustered DNA lesions. To repair them the cooperation of different DNA repair systems is required in the process of damage recognition and removal. This review is focused on the features of repair mechanisms for DNA with bulky lesions appeared in the result of action of natural carcinogen benzo[a]pyrene as an example.


Assuntos
Poluentes Atmosféricos/toxicidade , Dano ao DNA/efeitos dos fármacos , Reparo do DNA/genética , Hidrocarbonetos Policíclicos Aromáticos/toxicidade , Benzo(a)pireno/toxicidade , Adutos de DNA/efeitos dos fármacos , Reparo do DNA/efeitos dos fármacos , Humanos
9.
Biochemistry (Mosc) ; 77(4): 346-53, 2012 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-22809153

RESUMO

We have examined the influence of centrin 2 (Cen2) on the interaction of nucleotide excision repair factors (XPC-HR23b, RPA, and XPA) with 48-mer DNA duplexes bearing the dUMP derivative 5-{3-[6-(carboxyamidofluoresceinyl)amidocapromoyl]allyl}-2'-deoxyuridine-5'-monophosphate. The fluorescein residue linked to the nucleotide base imitates a bulky lesion of DNA. Cen2 stimulated the binding and increased the yield of DNA adducts with XPC-HR23b, a protein recognizing bulky damages in DNA. Stimulation of the binding was most pronounced in the presence of Mg(2+) and demonstrated a bell-shaped dependence on Cen2 concentration. The addition of Cen2 changed the stoichiometry of RPA-DNA complexes and diminished the yield of RPA-DNA covalent crosslinks. We have shown that Cen2 influences the binding of RPA and XPA with DNA, which results in formation of additional DNA-protein complexes possibly including Cen2. We have also found some evidence of direct contacts between Cen2 and DNA. These results in concert with the literature data suggest that Cen2 can be a regulatory element in the nucleotide excision repair system.


Assuntos
Proteínas de Ligação ao Cálcio/metabolismo , Proteínas de Ciclo Celular/metabolismo , Dano ao DNA , Reparo do DNA , DNA/metabolismo , Proteínas de Ligação ao Cálcio/genética , Proteínas de Ciclo Celular/genética , DNA/genética , Enzimas Reparadoras do DNA/genética , Enzimas Reparadoras do DNA/metabolismo , Proteínas de Ligação a DNA/genética , Proteínas de Ligação a DNA/metabolismo , Humanos , Ligação Proteica , Proteína de Replicação A/genética , Proteína de Replicação A/metabolismo , Proteína de Xeroderma Pigmentoso Grupo A/genética , Proteína de Xeroderma Pigmentoso Grupo A/metabolismo
10.
Biochemistry (Mosc) ; 77(5): 524-31, 2012 May.
Artigo em Inglês | MEDLINE | ID: mdl-22813594

RESUMO

The interaction of nucleotide excision repair (NER) proteins (XPC-HR23b, RPA, and XPA) with 48-mer DNA duplexes containing the bulky lesion-mimicking fluorescein-substituted derivative of dUMP (5-{3-[6-(carboxyamidofluoresceinyl)amidocapromoyl]allyl}-2'-deoxyuridine-5'-monophosphate) in a cluster with a lesion of another type (apurinic/apyrimidinic (AP) site) has been studied. It is shown that XPC-HR23b is modified to a greater extent by the DNA duplex containing an AP site opposite nucleotide adjacent to the fluorescein residue than by DNA containing an AP site shifted to the 3'- or 5'-end of the DNA strand. The efficiency of XPA modification by DNA duplexes containing both AP site and fluorescein residue is higher than that by DNA lacking the bulky lesion; the modification pattern in this case depends on the AP site position. In accordance with its major function, RPA interacts more efficiently with single-stranded DNA than with DNA duplexes, including those bearing bulky lesions. The observed interaction between the proteins involved in nucleotide excision repair and DNA structures containing a bulky lesion processed by NER and the AP site repaired via base excision repair may be significant for both these repair pathways in cells and requires the specific sequence of repair of clustered DNA lesions.


Assuntos
Reparo do DNA , DNA/metabolismo , Proteína de Replicação A/metabolismo , Proteína de Xeroderma Pigmentoso Grupo A/metabolismo , Sequência de Bases , DNA/química , DNA de Cadeia Simples/metabolismo , Nucleotídeos de Desoxiuracil/química , Nucleotídeos de Desoxiuracil/metabolismo , Dimerização , Fluoresceínas/química , Humanos , Conformação de Ácido Nucleico , Ligação Proteica , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Proteína de Replicação A/genética , Proteína de Xeroderma Pigmentoso Grupo A/genética
11.
Biochemistry (Mosc) ; 76(1): 24-35, 2011 Jan.
Artigo em Inglês | MEDLINE | ID: mdl-21568837

RESUMO

Nucleotide excision repair (NER) is one of the major DNA repair pathways in eukaryotic cells counteracting genetic changes caused by DNA damage. NER removes a wide set of structurally diverse lesions such as pyrimidine dimers arising upon UV irradiation and bulky chemical adducts arising upon exposure to carcinogens or chemotherapeutic drugs. NER defects lead to severe diseases including some forms of cancer. In view of the broad substrate specificity of NER, it is of interest to understand how a certain set of proteins recognizes various DNA lesions in the context of a large excess of intact DNA. This review focuses on DNA damage recognition and following stages resulting in preincision complex assembly, the key and still most unclear steps of NER. The major models of primary damage recognition and preincision complex assembly are considered. The contribution of affinity labeling techniques in study of this process is discussed.


Assuntos
Dano ao DNA , Reparo do DNA , Proteínas de Ligação a DNA/metabolismo , Células Eucarióticas/metabolismo , Animais , DNA/genética , DNA/metabolismo , Proteínas de Ligação a DNA/genética , Humanos
12.
Subcell Biochem ; 50: 251-77, 2010.
Artigo em Inglês | MEDLINE | ID: mdl-20012586

RESUMO

Nucleotide excision repair (NER) is one of the major DNA repair pathways in eukaryotic cells that counteract the formation of genetic damage. NER removes structurally diverse lesions such as pyrimidine dimers, arising upon UV irradiation, and bulky chemical adducts, arising upon exposure to carcinogens and some chemotherapeutic drugs. NER defects lead to severe diseases, including some forms of cancer. In view of the broad substrate specificity of NER, it is of interest to understand how a certain set of proteins recognizes various DNA lesions in the contest of a large excess of intact DNA. This review focuses on DNA damage recognition, the key and, as yet, most questionable step of NER. Understanding of mechanism of this step of NER may give a key contribution to study of similar processes of DNA damage recognition (base excision repair, mismatch repair) and regulation of assembly of various DNA repair machines. The major models of primary damage recognition and pre-incision complex assembly are considered. The model of a sequential loading of repair proteins on damaged DNA seems most reasonable in the light of the available data. The possible contribution of affinity labeling technique in study of this process is discussed.


Assuntos
Dano ao DNA , Reparo do DNA , Genoma
14.
Biochemistry (Mosc) ; 74(11): 1278-84, 2009 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-19916945

RESUMO

The interaction of human recombinant DNA topoisomerase 1 (Top1) with linear and circular DNA structures containing a nick or short gap but lacking a specific Top1 recognition site was studied. The effect of key excision repair proteins on formation of the Top1 covalent adduct with the DNA repair intermediates was shown. Partial inhibition of the Top1-DNA-adduct formation upon addition of poly(ADP-ribose) polymerase 1 in the absence of NAD+ was shown, whereas in the presence of NAD+ formation of a high molecular weight product, most likely corresponding to poly(ADP)-ribosylated Top1-DNA adduct, was observed. The data show that the key base excision repair proteins can influence formation of suicide Top1-DNA adducts. Top1 was identified by immunoprecipitation in the bovine testis nuclear extract as the protein forming the main modification product with nick-containing DNA.


Assuntos
Adutos de DNA/metabolismo , Reparo do DNA , DNA Topoisomerases Tipo I/metabolismo , Poli(ADP-Ribose) Polimerases/metabolismo , Animais , Bovinos , Adutos de DNA/química , Adutos de DNA/genética , DNA Topoisomerases Tipo I/genética , Humanos , Masculino , Poli(ADP-Ribose) Polimerase-1 , Poli(ADP-Ribose) Polimerases/genética , Ligação Proteica , Testículo/química , Testículo/metabolismo
16.
Biochemistry (Mosc) ; 73(11): 1207-13, 2008 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-19120024

RESUMO

The main strategy used by pro- and eukaryotic cells for replication of damaged DNA is translesion synthesis (TLS). Here, we investigate the TLS process catalyzed by DNA polymerases beta and lambda on DNA substrates using mono- or dinucleotide gaps opposite damage located in the template strand. An analog of a natural apurinic/apyrimidinic site, the 3-hydroxy-2-hydroxymetylthetrahydrofuran residue (THF), was used as damage. DNA was synthesized in the presence of either Mg2+ or Mn2+. DNA polymerases beta and lambda were able to catalyze DNA synthesis across THF only in the presence of Mn2+. Moreover, strand displacement synthesis was not observed. The primer was elongated by only one nucleotide. Another unusual aspect of the synthesis is that dTTP could not serve as a substrate in all cases. dATP was a preferential substrate for synthesis catalyzed by DNA polymerase beta. As for DNA polymerase lambda, dGMP was the only incorporated nucleotide out of four investigated. Modified on heterocyclic base photoreactive analogs of dCTP and dUTP showed substrate specificity for DNA polymerase beta. In contrast, the dCTP analog modified on the exocyclic amino group was a substrate for DNA polymerase lambda. We also observed that human replication protein A inhibited polymerase incorporation by both DNA polymerases beta and lambda on DNA templates containing damage.


Assuntos
DNA Polimerase beta/metabolismo , Replicação do DNA , DNA Polimerase beta/química , DNA Polimerase beta/genética , Reparo do DNA , Desoxirribonucleotídeos/metabolismo , Genoma , Humanos , Cinética , Especificidade por Substrato , Moldes Genéticos
17.
Mol Biol (Mosk) ; 42(1): 24-31, 2008.
Artigo em Russo | MEDLINE | ID: mdl-18389616

RESUMO

Nucleotide excision repair is one of the most important pathways of DNA repair in eukaryotic cells. Defects of this system lead to serious diseases including certain kinds of cancer. Nucleotide excision repair is able to remove a wide range of the structurally diverse DNA damages such as UV induced pyrimidine dimers, bulky chemical adducts arising under the action of carcinogenic compounds or chemotherapeutical drugs on cellular DNA. A broad substrate specificity of this repair pathway is related to the main intriguing question that is the mechanism of damage recognition by the protein complex in the context of the large excess of undamaged DNA. This review is detailed on the key stage of nucleotide excision repair--the recognition of a lesion in DNA, which is still most debated. We have considered the main models of a primary damage recognition and preincision complex formation that have been suggested by the leading groups in this field. Data presented allow to suggest the model of sequential loading of the proteins of reparative complex on damage DNA as the most reasonable.


Assuntos
Dano ao DNA/fisiologia , Reparo do DNA/fisiologia , Modelos Biológicos , Animais , Carcinógenos/toxicidade , Dano ao DNA/efeitos dos fármacos , Dano ao DNA/efeitos da radiação , Reparo do DNA/efeitos dos fármacos , Reparo do DNA/efeitos da radiação , Células Eucarióticas/fisiologia , Humanos , Complexos Multiproteicos/metabolismo , Neoplasias/metabolismo , Dímeros de Pirimidina/metabolismo , Raios Ultravioleta/efeitos adversos
18.
Biochim Biophys Acta ; 1172(1-2): 89-94, 1993 Feb 20.
Artigo em Inglês | MEDLINE | ID: mdl-8439575

RESUMO

We describe the properties of two new restriction endonucleases VspI and Tru9I which recognize sequences AT TAAT and T TAA, respectively. The molecular weights, subunit structure and steady-state kinetic constants of these enzymes for native and modified substrates have been determined. We have investigated the interaction of VspI and Tru9I with synthetic oligonucleotides containing modifications either within the recognition sites or around them. These modifications represent the substitution of different DNA deoxyribonucleosides by 1,2-dideoxy-D-ribofuranose, which corresponds to loss of the heterocyclic base while the sugar-phosphate chain remains intact. The effects of the substitutions were analyzed by determining the steady-state kinetic values of the hydrolysis reaction by VspI and Tru9I. The enzymes exhibited Michaelis-Menten kinetics for hydrolyzable substrates. The initial rates (V0) of hydrolysis of modified and unmodified strands of the duplexes varied as a result of these substitutions. The substrates for VspI and Tru9I which contain modifications around the bond to be hydrolyzed or within the complementary nucleosides were unreactive.


Assuntos
DNA/metabolismo , Desoxirribonucleases de Sítio Específico do Tipo II/metabolismo , Oligodesoxirribonucleotídeos/metabolismo , Sequência de Bases , Cinética , Dados de Sequência Molecular , Peso Molecular , Oligodesoxirribonucleotídeos/síntese química , Especificidade por Substrato , Termodinâmica
20.
Gene ; 157(1-2): 65-6, 1995 May 19.
Artigo em Inglês | MEDLINE | ID: mdl-7607528

RESUMO

The gene (vspIM) encoding VspI methyltransferase (MTase) has previously been cloned and sequenced, and shown to belong to the gamma class of m6-adenine MTases [Degtyarev et al., Nucleic Acids Res. 21 (1993) 2015]. Here it is shown that the MTase modifies the third adenine within the recognition sequence 5'-ATTAAT-3'.


Assuntos
DNA Metiltransferases Sítio Específica (Adenina-Específica)/genética , DNA Metiltransferases Sítio Específica (Adenina-Específica)/metabolismo , Sequência de Bases , Clonagem Molecular/métodos , Genes Bacterianos , Cinética , Dados de Sequência Molecular , Proteínas Recombinantes/biossíntese , Proteínas Recombinantes/metabolismo , DNA Metiltransferases Sítio Específica (Adenina-Específica)/biossíntese , Especificidade por Substrato
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