A DNA-modification methylase from Bacillus stearothermophilus V

R. Barra; M. Chiong; E. Gonzalez; C. Vasquez

A DNA-modification methylase from Bacillus stearothermophilus V

R. Barra, M. Chiong, E. Gonzalez, C. Vasquez

Universidad de Chile

Research output: Contribution to journal › Article › peer-review

13 Citations (Scopus)

Abstract

A type II modification methylase (M BstVI) was partially purified from the thermophilic bacterium Bacillus stearothermophilus V. The methylase catalyses the transfer of methyl groups from S-adenosyl-L-methionine to unmodified double-stranded DNA. The product of methylation was identified by paper chromatography as N⁶-methyladenine. Since M BstVI protects DNA against cleavage by BstVI and XhoI restriction endonucleases, it follows that it methylates the adenine residue in the sequence 5'-C-T-C-G-A-G-3'.

Original language	English
Pages (from-to)	699-703
Number of pages	5
Journal	Biochemical Journal
Volume	255
Issue number	2
Publication status	Published - 1988

ASJC Scopus Subject Areas

Biochemistry
Molecular Biology
Cell Biology

Cite this

Barra, R., Chiong, M., Gonzalez, E., & Vasquez, C. (1988). A DNA-modification methylase from Bacillus stearothermophilus V. Biochemical Journal, 255(2), 699-703.

@article{901f6fb5377142cca60e4ea5fd3fada3,

title = "A DNA-modification methylase from Bacillus stearothermophilus V",

abstract = "A type II modification methylase (M BstVI) was partially purified from the thermophilic bacterium Bacillus stearothermophilus V. The methylase catalyses the transfer of methyl groups from S-adenosyl-L-methionine to unmodified double-stranded DNA. The product of methylation was identified by paper chromatography as N6-methyladenine. Since M BstVI protects DNA against cleavage by BstVI and XhoI restriction endonucleases, it follows that it methylates the adenine residue in the sequence 5'-C-T-C-G-A-G-3'.",

author = "R. Barra and M. Chiong and E. Gonzalez and C. Vasquez",

year = "1988",

language = "English",

volume = "255",

pages = "699--703",

journal = "Biochemical Journal",

issn = "0264-6021",

publisher = "Portland Press Ltd.",

number = "2",

}

TY - JOUR

T1 - A DNA-modification methylase from Bacillus stearothermophilus V

AU - Barra, R.

AU - Chiong, M.

AU - Gonzalez, E.

AU - Vasquez, C.

PY - 1988

Y1 - 1988

N2 - A type II modification methylase (M BstVI) was partially purified from the thermophilic bacterium Bacillus stearothermophilus V. The methylase catalyses the transfer of methyl groups from S-adenosyl-L-methionine to unmodified double-stranded DNA. The product of methylation was identified by paper chromatography as N6-methyladenine. Since M BstVI protects DNA against cleavage by BstVI and XhoI restriction endonucleases, it follows that it methylates the adenine residue in the sequence 5'-C-T-C-G-A-G-3'.

AB - A type II modification methylase (M BstVI) was partially purified from the thermophilic bacterium Bacillus stearothermophilus V. The methylase catalyses the transfer of methyl groups from S-adenosyl-L-methionine to unmodified double-stranded DNA. The product of methylation was identified by paper chromatography as N6-methyladenine. Since M BstVI protects DNA against cleavage by BstVI and XhoI restriction endonucleases, it follows that it methylates the adenine residue in the sequence 5'-C-T-C-G-A-G-3'.

UR - http://www.scopus.com/inward/record.url?scp=0023707686&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023707686&partnerID=8YFLogxK

M3 - Article

C2 - 3202841

AN - SCOPUS:0023707686

SN - 0264-6021

VL - 255

SP - 699

EP - 703

JO - Biochemical Journal

JF - Biochemical Journal

IS - 2

ER -

A DNA-modification methylase from Bacillus stearothermophilus V

Abstract

ASJC Scopus Subject Areas

Other files and links

Fingerprint

Cite this