Salt in surroundings influences the production of serine protease into milieu by Aeromonas sobria

Rasel Khan, Eizo Takahashi, Thandavarayan Ramamurthy, Yoshifumi Takeda, Keinosuke Okamoto

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Previously we have shown that the open reading frame 2 protein (ORF2 protein), which is encoded at the 3′ end of serine protease of Aeromonas sobria (ASP), functions as a chaperone protein in periplasm in the production of ASP. Both proteins, ASP and ORF2 protein, associate in periplasm and ORF2 protein helps ASP to take an active form. ASP which is dissociated from ORF2 protein emerges in milieu. In this study, we examined the effect of sodium chloride (NaCl) in medium on ASP production by A. sobria. The ASP activity of culture supernatant was extremely decreased when A. sobria was cultured in medium containing 3.0% NaCl (concentration almost equivalent to sea water salinity). Our analysis showed that the transcription of asp by A. sobria is not inhibited by NaCl in medium and that A. sobria synthesizes and releases ASP in milieu even under the condition of 3.0% NaCl. However, these ASPs in milieu formed complex as with ORF2 proteins. This indicates that the maturation pathway of ASP is disturbed in A. sobria cultured in medium containing 3.0% NaCl. It is likely that ASP does not associate with ORF2 protein in the correct form in periplasam when A. sobria is cultured in medium containing 3.0% NaCl, though both proteins, ASP and ORF2 protein, make complexes and emerge outside of the cell. This idea suggests that the chaperone system of ASP possesses the ability to sense NaCl in surroundings and regulates the production of active ASP.

Original languageEnglish
Pages (from-to)963-976
Number of pages14
JournalMicrobiology and Immunology
Volume51
Issue number10
Publication statusPublished - 2007

Fingerprint

Aeromonas
Serine Proteases
Salts
Open Reading Frames
Proteins
Periplasm
Salinity
Seawater
Viperidae
Sodium Chloride

Keywords

  • Aeromonas sobria
  • Chaperone
  • Salt
  • Serine protease

ASJC Scopus subject areas

  • Immunology and Microbiology(all)
  • Microbiology (medical)
  • Microbiology

Cite this

Salt in surroundings influences the production of serine protease into milieu by Aeromonas sobria. / Khan, Rasel; Takahashi, Eizo; Ramamurthy, Thandavarayan; Takeda, Yoshifumi; Okamoto, Keinosuke.

In: Microbiology and Immunology, Vol. 51, No. 10, 2007, p. 963-976.

Research output: Contribution to journalArticle

@article{b2b76a72409848899fbe0ce10ae1bdc5,
title = "Salt in surroundings influences the production of serine protease into milieu by Aeromonas sobria",
abstract = "Previously we have shown that the open reading frame 2 protein (ORF2 protein), which is encoded at the 3′ end of serine protease of Aeromonas sobria (ASP), functions as a chaperone protein in periplasm in the production of ASP. Both proteins, ASP and ORF2 protein, associate in periplasm and ORF2 protein helps ASP to take an active form. ASP which is dissociated from ORF2 protein emerges in milieu. In this study, we examined the effect of sodium chloride (NaCl) in medium on ASP production by A. sobria. The ASP activity of culture supernatant was extremely decreased when A. sobria was cultured in medium containing 3.0{\%} NaCl (concentration almost equivalent to sea water salinity). Our analysis showed that the transcription of asp by A. sobria is not inhibited by NaCl in medium and that A. sobria synthesizes and releases ASP in milieu even under the condition of 3.0{\%} NaCl. However, these ASPs in milieu formed complex as with ORF2 proteins. This indicates that the maturation pathway of ASP is disturbed in A. sobria cultured in medium containing 3.0{\%} NaCl. It is likely that ASP does not associate with ORF2 protein in the correct form in periplasam when A. sobria is cultured in medium containing 3.0{\%} NaCl, though both proteins, ASP and ORF2 protein, make complexes and emerge outside of the cell. This idea suggests that the chaperone system of ASP possesses the ability to sense NaCl in surroundings and regulates the production of active ASP.",
keywords = "Aeromonas sobria, Chaperone, Salt, Serine protease",
author = "Rasel Khan and Eizo Takahashi and Thandavarayan Ramamurthy and Yoshifumi Takeda and Keinosuke Okamoto",
year = "2007",
language = "English",
volume = "51",
pages = "963--976",
journal = "Microbiology and Immunology",
issn = "0385-5600",
publisher = "Center for Academic Publications Japan",
number = "10",

}

TY - JOUR

T1 - Salt in surroundings influences the production of serine protease into milieu by Aeromonas sobria

AU - Khan, Rasel

AU - Takahashi, Eizo

AU - Ramamurthy, Thandavarayan

AU - Takeda, Yoshifumi

AU - Okamoto, Keinosuke

PY - 2007

Y1 - 2007

N2 - Previously we have shown that the open reading frame 2 protein (ORF2 protein), which is encoded at the 3′ end of serine protease of Aeromonas sobria (ASP), functions as a chaperone protein in periplasm in the production of ASP. Both proteins, ASP and ORF2 protein, associate in periplasm and ORF2 protein helps ASP to take an active form. ASP which is dissociated from ORF2 protein emerges in milieu. In this study, we examined the effect of sodium chloride (NaCl) in medium on ASP production by A. sobria. The ASP activity of culture supernatant was extremely decreased when A. sobria was cultured in medium containing 3.0% NaCl (concentration almost equivalent to sea water salinity). Our analysis showed that the transcription of asp by A. sobria is not inhibited by NaCl in medium and that A. sobria synthesizes and releases ASP in milieu even under the condition of 3.0% NaCl. However, these ASPs in milieu formed complex as with ORF2 proteins. This indicates that the maturation pathway of ASP is disturbed in A. sobria cultured in medium containing 3.0% NaCl. It is likely that ASP does not associate with ORF2 protein in the correct form in periplasam when A. sobria is cultured in medium containing 3.0% NaCl, though both proteins, ASP and ORF2 protein, make complexes and emerge outside of the cell. This idea suggests that the chaperone system of ASP possesses the ability to sense NaCl in surroundings and regulates the production of active ASP.

AB - Previously we have shown that the open reading frame 2 protein (ORF2 protein), which is encoded at the 3′ end of serine protease of Aeromonas sobria (ASP), functions as a chaperone protein in periplasm in the production of ASP. Both proteins, ASP and ORF2 protein, associate in periplasm and ORF2 protein helps ASP to take an active form. ASP which is dissociated from ORF2 protein emerges in milieu. In this study, we examined the effect of sodium chloride (NaCl) in medium on ASP production by A. sobria. The ASP activity of culture supernatant was extremely decreased when A. sobria was cultured in medium containing 3.0% NaCl (concentration almost equivalent to sea water salinity). Our analysis showed that the transcription of asp by A. sobria is not inhibited by NaCl in medium and that A. sobria synthesizes and releases ASP in milieu even under the condition of 3.0% NaCl. However, these ASPs in milieu formed complex as with ORF2 proteins. This indicates that the maturation pathway of ASP is disturbed in A. sobria cultured in medium containing 3.0% NaCl. It is likely that ASP does not associate with ORF2 protein in the correct form in periplasam when A. sobria is cultured in medium containing 3.0% NaCl, though both proteins, ASP and ORF2 protein, make complexes and emerge outside of the cell. This idea suggests that the chaperone system of ASP possesses the ability to sense NaCl in surroundings and regulates the production of active ASP.

KW - Aeromonas sobria

KW - Chaperone

KW - Salt

KW - Serine protease

UR - http://www.scopus.com/inward/record.url?scp=35448956741&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=35448956741&partnerID=8YFLogxK

M3 - Article

C2 - 17951986

AN - SCOPUS:35448956741

VL - 51

SP - 963

EP - 976

JO - Microbiology and Immunology

JF - Microbiology and Immunology

SN - 0385-5600

IS - 10

ER -