Sequence analysis of the Legionella micdadei groELS operon

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Sequence analysis of the Legionella micdadei groELS operon. / Hindersson, P; Høiby, N; Bangsborg, Jette Marie.

In: F E M S Microbiology Letters, Vol. 61, No. 1, 1991, p. 31-8.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Hindersson, P, Høiby, N & Bangsborg, JM 1991, 'Sequence analysis of the Legionella micdadei groELS operon', F E M S Microbiology Letters, vol. 61, no. 1, pp. 31-8.

APA

Hindersson, P., Høiby, N., & Bangsborg, J. M. (1991). Sequence analysis of the Legionella micdadei groELS operon. F E M S Microbiology Letters, 61(1), 31-8.

Vancouver

Hindersson P, Høiby N, Bangsborg JM. Sequence analysis of the Legionella micdadei groELS operon. F E M S Microbiology Letters. 1991;61(1):31-8.

Author

Hindersson, P ; Høiby, N ; Bangsborg, Jette Marie. / Sequence analysis of the Legionella micdadei groELS operon. In: F E M S Microbiology Letters. 1991 ; Vol. 61, No. 1. pp. 31-8.

Bibtex

@article{5e8ae4cc5d4f457dbfd8466fbb5b2328,
title = "Sequence analysis of the Legionella micdadei groELS operon",
abstract = "A 2.7 kb DNA fragment encoding the 60 kDa common antigen (CA) and a 13 kDa protein of Legionella micdadei was sequenced. Two open reading frames of 57,677 and 10,456 Da were identified, corresponding to the heat shock proteins GroEL and GroES, respectively. Typical -35, -10, and Shine-Dalgarno heat shock expression signals were identified upstream of the L. micdadei groEL gene. Further upstream, a poly-T region, also a feature of the sigma 32-regulated Escherichia coli groELS heat shock operon, was found. Despite the high degree of homology of the expression signals in E. coli and L. micdadei, Western blot analysis with an L. micdadei specific anti-groEL antibody did not reveal a significant increase in the amount of the GroEL protein during heat shock in L. micdadei or in the recombinant E. coli expressing L. micdadei GroEL.",
keywords = "Amino Acid Sequence, Bacterial Proteins, Base Sequence, Chaperonin 60, DNA, Bacterial, Escherichia coli, Gene Expression Regulation, Bacterial, Heat-Shock Proteins, Legionella, Molecular Sequence Data, Molecular Weight, Open Reading Frames, Operon, Regulatory Sequences, Nucleic Acid, Restriction Mapping, Sequence Homology, Nucleic Acid",
author = "P Hindersson and N H{\o}iby and Bangsborg, {Jette Marie}",
year = "1991",
language = "English",
volume = "61",
pages = "31--8",
journal = "F E M S Microbiology Letters",
issn = "0378-1097",
publisher = "Oxford University Press",
number = "1",

}

RIS

TY - JOUR

T1 - Sequence analysis of the Legionella micdadei groELS operon

AU - Hindersson, P

AU - Høiby, N

AU - Bangsborg, Jette Marie

PY - 1991

Y1 - 1991

N2 - A 2.7 kb DNA fragment encoding the 60 kDa common antigen (CA) and a 13 kDa protein of Legionella micdadei was sequenced. Two open reading frames of 57,677 and 10,456 Da were identified, corresponding to the heat shock proteins GroEL and GroES, respectively. Typical -35, -10, and Shine-Dalgarno heat shock expression signals were identified upstream of the L. micdadei groEL gene. Further upstream, a poly-T region, also a feature of the sigma 32-regulated Escherichia coli groELS heat shock operon, was found. Despite the high degree of homology of the expression signals in E. coli and L. micdadei, Western blot analysis with an L. micdadei specific anti-groEL antibody did not reveal a significant increase in the amount of the GroEL protein during heat shock in L. micdadei or in the recombinant E. coli expressing L. micdadei GroEL.

AB - A 2.7 kb DNA fragment encoding the 60 kDa common antigen (CA) and a 13 kDa protein of Legionella micdadei was sequenced. Two open reading frames of 57,677 and 10,456 Da were identified, corresponding to the heat shock proteins GroEL and GroES, respectively. Typical -35, -10, and Shine-Dalgarno heat shock expression signals were identified upstream of the L. micdadei groEL gene. Further upstream, a poly-T region, also a feature of the sigma 32-regulated Escherichia coli groELS heat shock operon, was found. Despite the high degree of homology of the expression signals in E. coli and L. micdadei, Western blot analysis with an L. micdadei specific anti-groEL antibody did not reveal a significant increase in the amount of the GroEL protein during heat shock in L. micdadei or in the recombinant E. coli expressing L. micdadei GroEL.

KW - Amino Acid Sequence

KW - Bacterial Proteins

KW - Base Sequence

KW - Chaperonin 60

KW - DNA, Bacterial

KW - Escherichia coli

KW - Gene Expression Regulation, Bacterial

KW - Heat-Shock Proteins

KW - Legionella

KW - Molecular Sequence Data

KW - Molecular Weight

KW - Open Reading Frames

KW - Operon

KW - Regulatory Sequences, Nucleic Acid

KW - Restriction Mapping

KW - Sequence Homology, Nucleic Acid

M3 - Journal article

C2 - 1672279

VL - 61

SP - 31

EP - 38

JO - F E M S Microbiology Letters

JF - F E M S Microbiology Letters

SN - 0378-1097

IS - 1

ER -

ID: 40334306