Zobrazeno 1 - 10
of 14
pro vyhledávání: '"L. N. Golikova"'
Publikováno v:
Molecular Biology. 38:850-856
The Streptococcus faecalis ND547 and Bacillus stearothermophilus 19 genes that code for DNA methyltransferases (MTases, M.) of restriction–modification (RM) systems with the same recognition sequence, 5′-GCATC-3′ were cloned and sequenced. The
Autor:
S. Kh. Degtyarev, D. A. Gonchar, L. N. Golikova, N. A. Netesova, Abdurashitov Ma, Yu. G. Kashirina, Valery A Chernukhin
Publikováno v:
Biochemistry (Moscow). 68:967-975
The BstF5I restriction–modification system from Bacillus stearothermophilus F5 includes four site-specific DNA methyltransferases, thus differing from all known restriction–modification systems. Here we demonstrated for the first time that one ba
Autor:
S. Kh. Degtyarev, D. A. Gonchar, L. N. Golikova, N. A. Netesova, Abdurashitov Ma, S. S. Okhapkina
Publikováno v:
Molecular Biology. 37:524-528
The nucleotide sequence was established for the full-length Flavobacterium aquatile operon coding for the FauI restriction–modification system. The operon is unusual in structure and has the gene order control protein / DNA methyltransferase A / re
Autor:
N. A. Netesova, S. V. Sosnovtsev, Abdurashitov Ma, E. V. Seregina, S. Kh. Degtyarev, L. N. Golikova, S. S. Okhapkina
Publikováno v:
Molecular Biology. 36:333-337
A fragment containing the SfeI restriction–modification system (RMS) operon was cloned from a Streptococcus faecalis SE72 plasmid. Nucleotide sequence analysis revealed its high (99.2%) homology to the operon for Lactococcus lactis subsp. cremoris
Autor:
A. A. Evdokimov, N. S. Gololobova, Ernst G. Malygin, N. A. Netesova, S. Kh. Degtyarev, D. A. Gonchar, L. G. Ovetchkina, L. N. Golikova
Publikováno v:
Molecular Biology. 36:110-116
The BstF5I restriction-modification system from Bacillus stearothermophilus F5, unlike all known restriction-modification systems, contains three genes encoding DNA methyltransferases. In addition to revealing two DNA methylases responsible for modif
Autor:
N. A. Netesova, S. N. Shchelkunov, D. A. Gonchar, Gutorov Vv, S. Kh. Degtyarev, L. N. Golikova, S. S. Okhapkina, A. A. Evdokimov
Publikováno v:
Russian Journal of Bioorganic Chemistry. 28:77-79
The fourth DNA-methyltransferase of the BstF5I restriction–modification (RM) system from Bacillus stearothermophilus F5 (M.BstF5I-4) was discovered, which modifies the adenine residue within the upper strand of the recognition site 5"-GGATG-3"/5"-C
Autor:
V A, Chernukhin, L N, Golikova, D A, Gonchar, M A, Abdurashitov, Yu G, Kashirina, N A, Netesova, S Kh, Degtyarev
Publikováno v:
Biochemistry. Biokhimiia. 68(9)
The BstF5I restriction-modification system from Bacillus stearothermophilus F5 includes four site-specific DNA methyltransferases, thus differing from all known restriction-modification systems. Here we demonstrated for the first time that one bacter
Autor:
M A, Abdurashitov, S S, Okhapkina, N A, Netesova, L N, Golikova, D A, Gonchar, S Kh, Degtiarev
Publikováno v:
Molekuliarnaia biologiia. 37(4)
The nucleotide sequence was established for the full-length Flavobacterium aquatile operon coding for the FauI restriction-modification system. The operon is unusual in structure and has the gene order control protein gene-DNA methyltransferase A gen
Autor:
S S, Okhapkina, N A, Netesova, L N, Golikova, E V, Seregina, S V, Sosnovtsev, M A, Abdurashitov, S Kh, Degtiarev
Publikováno v:
Molekuliarnaia biologiia. 36(3)
A fragment containing the SfeI restriction-modification system (RMS) operon was cloned from a Streptococcus faecalis SE72 plasmid. Nucleotide sequence analysis revealed its high (99.2%) homology to the operon for Lactococcus lactis subsp. cremoris W5
Autor:
L N, Golikova, V V, Guturov, A A, Evdokimov, S N, Shchelkunov, D A, Gonchar, S S, Okhapkina, S Kh, Degtiarev, N A, Netesova
Publikováno v:
Bioorganicheskaia khimiia. 28(1)
The fourth DNA-methyltransferase of the BstF5I restriction-modification (RM) system from Bacillus stearothermophilus F5 (M.BstF5I-4) was discovered, which modifies the adenine residue within the upper strand of the recognition site 5'-GGATG-3'/5'-CAT