Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and
Bradyrhizobium japonicum USDA110, Encode Haloalkane
Dehalogenases with Novel Structures and Substrate Specificities

J 2005

Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities

SATO, Yukari, Marta MONINCOVÁ, Radka CHALOUPKOVÁ, Zbyněk PROKOP, Yoshiyuki OHTSUBO et. al.

Basic information

Original name

Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities

Name in Czech

Dva rhiyobiální Kkeny Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110,kódující haloalkán dehalogenázy s novou strukturou a substrátovou specifitou.

Authors

SATO, Yukari (392 Japan), Marta MONINCOVÁ (203 Czech Republic), Radka CHALOUPKOVÁ (203 Czech Republic), Zbyněk PROKOP (203 Czech Republic), Yoshiyuki OHTSUBO (392 Japan), Kiwamu MINAMISAWA (392 Japan), Masataka TSUDA (392 Japan), Jiří DAMBORSKÝ (203 Czech Republic, guarantor) and Yuji NAGATA (392 Japan)

Edition

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2005, 0099-2240

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

United States of America

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 3.818

RIV identification code

RIV/00216224:14310/05:00014120

Organization unit

Faculty of Science

UT WoS

000231165500030

Keywords in English

Haloalkane dehalogenases;rhizobial strains;Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110;

Abstract

ORIG CZ

V originále

Haloalkane dehalogenases are key enzymes for the degradation of halogenated aliphatic pollutants. Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, have open reading frames (ORFs), mlr5434 and blr1087, respectively, that encode putative haloalkane dehalogenase homologues. The crude extracts of Escherichia coli strains expressing mlr5434 and blr1087 showed the ability to dehalogenate 18 halogenated compounds, indicating that these ORFs indeed encode haloalkane dehalogenases. Therefore, these ORFs were referred to as dmlA (dehalogenase from Mesorhizobium loti) and dbjA (dehalogenase from Bradyrhizobium japonicum), respectively. The principal component analysis of the substrate specificities of various haloalkane dehalogenases clearly showed that DbjA and DmlA constitute a novel substrate specificity class with extraordinarily high activity towards beta-methylated compounds. Comparison of the circular dichroism spectra of DbjA and other dehalogenases strongly suggested that DbjA contains more alpha-helices than the other dehalogenases. The dehalogenase activity of resting cells and Northern blot analyses both revealed that the dmlA and dbjA genes were expressed under normal culture conditions in MAFF303099 and USDA110 stain cells, respectively.

In Czech

lánek popisuje izolaci dvou nových kmen-Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, žijících na koenech v japonských rostlin.

Links

MSM0021622413, plan (intention)

Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment

Citovat

SATO, Yukari, Marta MONINCOVÁ, Radka CHALOUPKOVÁ, Zbyněk PROKOP, Yoshiyuki OHTSUBO, Kiwamu MINAMISAWA, Masataka TSUDA, Jiří DAMBORSKÝ and Yuji NAGATA. Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities. APPLIED AND ENVIRONMENTAL MICROBIOLOGY. 2005, vol. 71, No 8, p. 43724379-43724386. ISSN 0099-2240.

@article{586887,
   author = {Sato, Yukari and Monincová, Marta and Chaloupková, Radka and Prokop, Zbyněk and Ohtsubo, Yoshiyuki and Minamisawa, Kiwamu and Tsuda, Masataka and Damborský, Jiří and Nagata, Yuji},
   article_number = {8},
   keywords = {Haloalkane dehalogenases;rhizobial strains;Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110;},
   language = {eng},
   issn = {0099-2240},
   journal = {APPLIED AND ENVIRONMENTAL MICROBIOLOGY},
   title = {Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities},
   url = {http://loschmidt.chemi.muni.cz/peg/pdf/aem05b.pdf},
   volume = {71},
   year = {2005}
}

TY  - JOUR
ID  - 586887
AU  - Sato, Yukari - Monincová, Marta - Chaloupková, Radka - Prokop, Zbyněk - Ohtsubo, Yoshiyuki - Minamisawa, Kiwamu - Tsuda, Masataka - Damborský, Jiří - Nagata, Yuji
PY  - 2005
TI  - Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities
JF  - APPLIED AND ENVIRONMENTAL MICROBIOLOGY
VL  - 71
IS  - 8
SP  - 43724379
EP  - 43724379
SN  - 00992240
KW  - Haloalkane dehalogenases;rhizobial strains;Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110;
UR  - http://loschmidt.chemi.muni.cz/peg/pdf/aem05b.pdf
N2  - Haloalkane dehalogenases are key enzymes for the degradation of halogenated aliphatic pollutants. Two rhizobial strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, have open reading frames (ORFs), mlr5434 and blr1087, respectively, that encode putative haloalkane dehalogenase homologues. The crude extracts of Escherichia coli strains expressing mlr5434 and blr1087 showed the ability to dehalogenate 18 halogenated compounds, indicating that these ORFs indeed encode haloalkane dehalogenases. Therefore, these ORFs were referred to as dmlA (dehalogenase from Mesorhizobium loti) and dbjA (dehalogenase from Bradyrhizobium japonicum), respectively. The principal component analysis of the substrate specificities of various haloalkane dehalogenases clearly showed that DbjA and DmlA constitute a novel substrate specificity class with extraordinarily high activity towards beta-methylated compounds. Comparison of the circular dichroism spectra of DbjA and other dehalogenases strongly suggested that DbjA contains more alpha-helices than the other dehalogenases. The dehalogenase activity of resting cells and Northern blot analyses both revealed that the dmlA and dbjA genes were expressed under normal culture conditions in MAFF303099 and USDA110 stain cells, respectively.
ER  -

SATO, Yukari, Marta MONINCOVÁ, Radka CHALOUPKOVÁ, Zbyněk PROKOP, Yoshiyuki OHTSUBO, Kiwamu MINAMISAWA, Masataka TSUDA, Jiří DAMBORSKÝ and Yuji NAGATA. Two Rhizobial Strains, Mesorhizobium loti MAFF303099 and Bradyrhizobium japonicum USDA110, Encode Haloalkane Dehalogenases with Novel Structures and Substrate Specificities. \textit{APPLIED AND ENVIRONMENTAL MICROBIOLOGY}. 2005, vol.~71, No~8, p.~43724379-43724386. ISSN~0099-2240.

Detailed Information on Publication Record