Salicylate degradation by a cold-adapted Pseudomonas sp

Eunsol Ahn, Ki Young Choi, Beom Sik Kang, Gerben J. Zylstra, Dockyu Kim, Eungbin Kim

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Pseudomonas sp. strain MC1 was characterized as a cold-adapted, naphthalene-degrading bacterium that is able to grow in a broad temperature range of 5–30°C. MC1 harbors a catabolic plasmid, designated pYIC1, which is almost identical to the archetypal NAH7 plasmid from the mesophilic bacterium Pseudomonas putida G7. On pYIC1, the catabolic genes for naphthalene degradation are clustered in two operons: nahAa-Ab-Ac-Ad-B-F-C-Q-E-D encoding the conversion of naphthalene to salicylate, and nahG-T-H-I-N-L-O-M-K-J encoding the conversion of salicylate through meta-cleavage pathway to pyruvate and acetyl CoA. NahH, the bona fide extradiol dioxygenase in MC1 salicylate metabolism, is thermolabile and is a cold-adapted enzyme. The thermal profiles of the NahH enzyme activities expressed in different hosts indicate the presence of a factor(s) or mechanism(s) to protect the thermolabile NahH enzyme (100% aa identity with MC1 counterpart) in G7. Overall, the results reported in the present work suggest that the thermolabile NahH might be a product of the cold-adaptation process of MC1 and thus contribute to the survival and growth ability of MC1 on salicylate and naphthalene in cold environments.

Original languageEnglish
Pages (from-to)417-424
Number of pages8
JournalAnnals of Microbiology
Volume67
Issue number6
DOIs
Publication statusPublished - 2017 Jun 1

Fingerprint

Salicylates
Pseudomonas
Plasmids
Enzymes
Bacteria
Pseudomonas putida
Acetyl Coenzyme A
Operon
Pyruvic Acid
Hot Temperature
Temperature
naphthalene
Growth
Genes

All Science Journal Classification (ASJC) codes

  • Applied Microbiology and Biotechnology

Cite this

Ahn, E., Choi, K. Y., Kang, B. S., Zylstra, G. J., Kim, D., & Kim, E. (2017). Salicylate degradation by a cold-adapted Pseudomonas sp. Annals of Microbiology, 67(6), 417-424. https://doi.org/10.1007/s13213-017-1273-3
Ahn, Eunsol ; Choi, Ki Young ; Kang, Beom Sik ; Zylstra, Gerben J. ; Kim, Dockyu ; Kim, Eungbin. / Salicylate degradation by a cold-adapted Pseudomonas sp. In: Annals of Microbiology. 2017 ; Vol. 67, No. 6. pp. 417-424.
@article{c458a87e0c4f4a1cab96bcb7ee01feff,
title = "Salicylate degradation by a cold-adapted Pseudomonas sp",
abstract = "Pseudomonas sp. strain MC1 was characterized as a cold-adapted, naphthalene-degrading bacterium that is able to grow in a broad temperature range of 5–30°C. MC1 harbors a catabolic plasmid, designated pYIC1, which is almost identical to the archetypal NAH7 plasmid from the mesophilic bacterium Pseudomonas putida G7. On pYIC1, the catabolic genes for naphthalene degradation are clustered in two operons: nahAa-Ab-Ac-Ad-B-F-C-Q-E-D encoding the conversion of naphthalene to salicylate, and nahG-T-H-I-N-L-O-M-K-J encoding the conversion of salicylate through meta-cleavage pathway to pyruvate and acetyl CoA. NahH, the bona fide extradiol dioxygenase in MC1 salicylate metabolism, is thermolabile and is a cold-adapted enzyme. The thermal profiles of the NahH enzyme activities expressed in different hosts indicate the presence of a factor(s) or mechanism(s) to protect the thermolabile NahH enzyme (100{\%} aa identity with MC1 counterpart) in G7. Overall, the results reported in the present work suggest that the thermolabile NahH might be a product of the cold-adaptation process of MC1 and thus contribute to the survival and growth ability of MC1 on salicylate and naphthalene in cold environments.",
author = "Eunsol Ahn and Choi, {Ki Young} and Kang, {Beom Sik} and Zylstra, {Gerben J.} and Dockyu Kim and Eungbin Kim",
year = "2017",
month = "6",
day = "1",
doi = "10.1007/s13213-017-1273-3",
language = "English",
volume = "67",
pages = "417--424",
journal = "Annals of Microbiology",
issn = "1590-4261",
publisher = "Springer Heidelberg",
number = "6",

}

Ahn, E, Choi, KY, Kang, BS, Zylstra, GJ, Kim, D & Kim, E 2017, 'Salicylate degradation by a cold-adapted Pseudomonas sp', Annals of Microbiology, vol. 67, no. 6, pp. 417-424. https://doi.org/10.1007/s13213-017-1273-3

Salicylate degradation by a cold-adapted Pseudomonas sp. / Ahn, Eunsol; Choi, Ki Young; Kang, Beom Sik; Zylstra, Gerben J.; Kim, Dockyu; Kim, Eungbin.

In: Annals of Microbiology, Vol. 67, No. 6, 01.06.2017, p. 417-424.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Salicylate degradation by a cold-adapted Pseudomonas sp

AU - Ahn, Eunsol

AU - Choi, Ki Young

AU - Kang, Beom Sik

AU - Zylstra, Gerben J.

AU - Kim, Dockyu

AU - Kim, Eungbin

PY - 2017/6/1

Y1 - 2017/6/1

N2 - Pseudomonas sp. strain MC1 was characterized as a cold-adapted, naphthalene-degrading bacterium that is able to grow in a broad temperature range of 5–30°C. MC1 harbors a catabolic plasmid, designated pYIC1, which is almost identical to the archetypal NAH7 plasmid from the mesophilic bacterium Pseudomonas putida G7. On pYIC1, the catabolic genes for naphthalene degradation are clustered in two operons: nahAa-Ab-Ac-Ad-B-F-C-Q-E-D encoding the conversion of naphthalene to salicylate, and nahG-T-H-I-N-L-O-M-K-J encoding the conversion of salicylate through meta-cleavage pathway to pyruvate and acetyl CoA. NahH, the bona fide extradiol dioxygenase in MC1 salicylate metabolism, is thermolabile and is a cold-adapted enzyme. The thermal profiles of the NahH enzyme activities expressed in different hosts indicate the presence of a factor(s) or mechanism(s) to protect the thermolabile NahH enzyme (100% aa identity with MC1 counterpart) in G7. Overall, the results reported in the present work suggest that the thermolabile NahH might be a product of the cold-adaptation process of MC1 and thus contribute to the survival and growth ability of MC1 on salicylate and naphthalene in cold environments.

AB - Pseudomonas sp. strain MC1 was characterized as a cold-adapted, naphthalene-degrading bacterium that is able to grow in a broad temperature range of 5–30°C. MC1 harbors a catabolic plasmid, designated pYIC1, which is almost identical to the archetypal NAH7 plasmid from the mesophilic bacterium Pseudomonas putida G7. On pYIC1, the catabolic genes for naphthalene degradation are clustered in two operons: nahAa-Ab-Ac-Ad-B-F-C-Q-E-D encoding the conversion of naphthalene to salicylate, and nahG-T-H-I-N-L-O-M-K-J encoding the conversion of salicylate through meta-cleavage pathway to pyruvate and acetyl CoA. NahH, the bona fide extradiol dioxygenase in MC1 salicylate metabolism, is thermolabile and is a cold-adapted enzyme. The thermal profiles of the NahH enzyme activities expressed in different hosts indicate the presence of a factor(s) or mechanism(s) to protect the thermolabile NahH enzyme (100% aa identity with MC1 counterpart) in G7. Overall, the results reported in the present work suggest that the thermolabile NahH might be a product of the cold-adaptation process of MC1 and thus contribute to the survival and growth ability of MC1 on salicylate and naphthalene in cold environments.

UR - http://www.scopus.com/inward/record.url?scp=85019751674&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85019751674&partnerID=8YFLogxK

U2 - 10.1007/s13213-017-1273-3

DO - 10.1007/s13213-017-1273-3

M3 - Article

AN - SCOPUS:85019751674

VL - 67

SP - 417

EP - 424

JO - Annals of Microbiology

JF - Annals of Microbiology

SN - 1590-4261

IS - 6

ER -