GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp.

Donna R. Hill, Thomas J. Belbin, Marc V. Thorsteinsson, Deeni Bassam, Susanne Brass, Anneliese Ernst, Peter Böger, Hans Paerl, Martin E. Mulligan, Malcolm Potts

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

The glbN gene of Nostoc commune UTEX 584 is juxtaposed to nifU and nifH, and it encodes a 12-kDa monomeric hemoglobin that binds oxygen with high affinity. In N. commune UTEX 584, maximum accumulation of GlbN occurred in both the heterocysts and vegetative cells of nitrogen-fixing cultures when the rate of oxygen evolution was repressed to less than 25 μmol of O2 mg of chlorophyll a-1 h-1. Accumulation of GlbN coincided with maximum synthesis of NifH and ferredoxin NADP+ oxidoreductase (PetH or FNR). A total of 41 strains of cyanobacteria, including 40 nitrogen fixers and representing 16 genera within all five sections of the cyanobacteria were screened for the presence of glbN or GlbN, glbN was present in five Nostoc strains in a single copy. Genomic DNAs from 11 other Nostoc and Anabaena strains, including Anabaena sp. strain PCC 7120, provided no hybridization signals with a glbN probe. A constitutively expressed, 18-kDa protein which cross-reacted strongly with GlbN antibodies was detected in four Anabaena and Nostoc strains and in Trichodesmium thiebautii. The nifU-nifH intergenic region of Nostoc sp. strain MUN 8820 was sequenced (1,229 bp) and was approximately 95% identical to the equivalent region in N. commune UTEX 584. Each strand of the DNA from the nifU-nifH intergenic regions of both strains has the potential to fold into secondary structures in which more than 50% of the bases are internally paired. Mobility shift assays confirmed that NtcA (BifA) bound a site in the nifU-glbN intergenic region of N. commune UTEX 584 approximately 100 bases upstream from the translation initiation site of glbN. This site showed extensive sequence similarity with the promoter region of glnA from Synechococcus sp. strain PCC 7942. In vivo, GlbN had a specific and prominent subcellular location around the periphery of the cytosolic face of the cell membrane, and the protein was found solely in the soluble fraction of cell extracts. Our hypothesis is that GlbN scavenges oxygen for and is a component of a membrane-associated microaerobically induced terminal cytochrome oxidase.

Original languageEnglish (US)
Pages (from-to)6587-6598
Number of pages12
JournalJournal of Bacteriology
Volume178
Issue number22
StatePublished - 1996
Externally publishedYes

Fingerprint

Nostoc commune
Nostoc
Anabaena
Intergenic DNA
Membrane Proteins
Cyanobacteria
Oxygen
Nitrogen
Ferredoxin-NADP Reductase
Synechococcus
DNA
Electrophoretic Mobility Shift Assay
Electron Transport Complex IV
Cell Extracts
Genetic Promoter Regions
Hemoglobins
Membranes
Antibodies
Genes
Proteins

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

Hill, D. R., Belbin, T. J., Thorsteinsson, M. V., Bassam, D., Brass, S., Ernst, A., ... Potts, M. (1996). GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp. Journal of Bacteriology, 178(22), 6587-6598.

GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp. / Hill, Donna R.; Belbin, Thomas J.; Thorsteinsson, Marc V.; Bassam, Deeni; Brass, Susanne; Ernst, Anneliese; Böger, Peter; Paerl, Hans; Mulligan, Martin E.; Potts, Malcolm.

In: Journal of Bacteriology, Vol. 178, No. 22, 1996, p. 6587-6598.

Research output: Contribution to journalArticle

Hill, DR, Belbin, TJ, Thorsteinsson, MV, Bassam, D, Brass, S, Ernst, A, Böger, P, Paerl, H, Mulligan, ME & Potts, M 1996, 'GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp.', Journal of Bacteriology, vol. 178, no. 22, pp. 6587-6598.
Hill DR, Belbin TJ, Thorsteinsson MV, Bassam D, Brass S, Ernst A et al. GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp. Journal of Bacteriology. 1996;178(22):6587-6598.
Hill, Donna R. ; Belbin, Thomas J. ; Thorsteinsson, Marc V. ; Bassam, Deeni ; Brass, Susanne ; Ernst, Anneliese ; Böger, Peter ; Paerl, Hans ; Mulligan, Martin E. ; Potts, Malcolm. / GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp. In: Journal of Bacteriology. 1996 ; Vol. 178, No. 22. pp. 6587-6598.
@article{888845bade784d2990539db07f04b0a7,
title = "GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp.",
abstract = "The glbN gene of Nostoc commune UTEX 584 is juxtaposed to nifU and nifH, and it encodes a 12-kDa monomeric hemoglobin that binds oxygen with high affinity. In N. commune UTEX 584, maximum accumulation of GlbN occurred in both the heterocysts and vegetative cells of nitrogen-fixing cultures when the rate of oxygen evolution was repressed to less than 25 μmol of O2 mg of chlorophyll a-1 h-1. Accumulation of GlbN coincided with maximum synthesis of NifH and ferredoxin NADP+ oxidoreductase (PetH or FNR). A total of 41 strains of cyanobacteria, including 40 nitrogen fixers and representing 16 genera within all five sections of the cyanobacteria were screened for the presence of glbN or GlbN, glbN was present in five Nostoc strains in a single copy. Genomic DNAs from 11 other Nostoc and Anabaena strains, including Anabaena sp. strain PCC 7120, provided no hybridization signals with a glbN probe. A constitutively expressed, 18-kDa protein which cross-reacted strongly with GlbN antibodies was detected in four Anabaena and Nostoc strains and in Trichodesmium thiebautii. The nifU-nifH intergenic region of Nostoc sp. strain MUN 8820 was sequenced (1,229 bp) and was approximately 95{\%} identical to the equivalent region in N. commune UTEX 584. Each strand of the DNA from the nifU-nifH intergenic regions of both strains has the potential to fold into secondary structures in which more than 50{\%} of the bases are internally paired. Mobility shift assays confirmed that NtcA (BifA) bound a site in the nifU-glbN intergenic region of N. commune UTEX 584 approximately 100 bases upstream from the translation initiation site of glbN. This site showed extensive sequence similarity with the promoter region of glnA from Synechococcus sp. strain PCC 7942. In vivo, GlbN had a specific and prominent subcellular location around the periphery of the cytosolic face of the cell membrane, and the protein was found solely in the soluble fraction of cell extracts. Our hypothesis is that GlbN scavenges oxygen for and is a component of a membrane-associated microaerobically induced terminal cytochrome oxidase.",
author = "Hill, {Donna R.} and Belbin, {Thomas J.} and Thorsteinsson, {Marc V.} and Deeni Bassam and Susanne Brass and Anneliese Ernst and Peter B{\"o}ger and Hans Paerl and Mulligan, {Martin E.} and Malcolm Potts",
year = "1996",
language = "English (US)",
volume = "178",
pages = "6587--6598",
journal = "Journal of Bacteriology",
issn = "0021-9193",
publisher = "American Society for Microbiology",
number = "22",

}

TY - JOUR

T1 - GlbN (cyanoglobin) is a peripheral membrane protein that is restricted to certain Nostoc spp.

AU - Hill, Donna R.

AU - Belbin, Thomas J.

AU - Thorsteinsson, Marc V.

AU - Bassam, Deeni

AU - Brass, Susanne

AU - Ernst, Anneliese

AU - Böger, Peter

AU - Paerl, Hans

AU - Mulligan, Martin E.

AU - Potts, Malcolm

PY - 1996

Y1 - 1996

N2 - The glbN gene of Nostoc commune UTEX 584 is juxtaposed to nifU and nifH, and it encodes a 12-kDa monomeric hemoglobin that binds oxygen with high affinity. In N. commune UTEX 584, maximum accumulation of GlbN occurred in both the heterocysts and vegetative cells of nitrogen-fixing cultures when the rate of oxygen evolution was repressed to less than 25 μmol of O2 mg of chlorophyll a-1 h-1. Accumulation of GlbN coincided with maximum synthesis of NifH and ferredoxin NADP+ oxidoreductase (PetH or FNR). A total of 41 strains of cyanobacteria, including 40 nitrogen fixers and representing 16 genera within all five sections of the cyanobacteria were screened for the presence of glbN or GlbN, glbN was present in five Nostoc strains in a single copy. Genomic DNAs from 11 other Nostoc and Anabaena strains, including Anabaena sp. strain PCC 7120, provided no hybridization signals with a glbN probe. A constitutively expressed, 18-kDa protein which cross-reacted strongly with GlbN antibodies was detected in four Anabaena and Nostoc strains and in Trichodesmium thiebautii. The nifU-nifH intergenic region of Nostoc sp. strain MUN 8820 was sequenced (1,229 bp) and was approximately 95% identical to the equivalent region in N. commune UTEX 584. Each strand of the DNA from the nifU-nifH intergenic regions of both strains has the potential to fold into secondary structures in which more than 50% of the bases are internally paired. Mobility shift assays confirmed that NtcA (BifA) bound a site in the nifU-glbN intergenic region of N. commune UTEX 584 approximately 100 bases upstream from the translation initiation site of glbN. This site showed extensive sequence similarity with the promoter region of glnA from Synechococcus sp. strain PCC 7942. In vivo, GlbN had a specific and prominent subcellular location around the periphery of the cytosolic face of the cell membrane, and the protein was found solely in the soluble fraction of cell extracts. Our hypothesis is that GlbN scavenges oxygen for and is a component of a membrane-associated microaerobically induced terminal cytochrome oxidase.

AB - The glbN gene of Nostoc commune UTEX 584 is juxtaposed to nifU and nifH, and it encodes a 12-kDa monomeric hemoglobin that binds oxygen with high affinity. In N. commune UTEX 584, maximum accumulation of GlbN occurred in both the heterocysts and vegetative cells of nitrogen-fixing cultures when the rate of oxygen evolution was repressed to less than 25 μmol of O2 mg of chlorophyll a-1 h-1. Accumulation of GlbN coincided with maximum synthesis of NifH and ferredoxin NADP+ oxidoreductase (PetH or FNR). A total of 41 strains of cyanobacteria, including 40 nitrogen fixers and representing 16 genera within all five sections of the cyanobacteria were screened for the presence of glbN or GlbN, glbN was present in five Nostoc strains in a single copy. Genomic DNAs from 11 other Nostoc and Anabaena strains, including Anabaena sp. strain PCC 7120, provided no hybridization signals with a glbN probe. A constitutively expressed, 18-kDa protein which cross-reacted strongly with GlbN antibodies was detected in four Anabaena and Nostoc strains and in Trichodesmium thiebautii. The nifU-nifH intergenic region of Nostoc sp. strain MUN 8820 was sequenced (1,229 bp) and was approximately 95% identical to the equivalent region in N. commune UTEX 584. Each strand of the DNA from the nifU-nifH intergenic regions of both strains has the potential to fold into secondary structures in which more than 50% of the bases are internally paired. Mobility shift assays confirmed that NtcA (BifA) bound a site in the nifU-glbN intergenic region of N. commune UTEX 584 approximately 100 bases upstream from the translation initiation site of glbN. This site showed extensive sequence similarity with the promoter region of glnA from Synechococcus sp. strain PCC 7942. In vivo, GlbN had a specific and prominent subcellular location around the periphery of the cytosolic face of the cell membrane, and the protein was found solely in the soluble fraction of cell extracts. Our hypothesis is that GlbN scavenges oxygen for and is a component of a membrane-associated microaerobically induced terminal cytochrome oxidase.

UR - http://www.scopus.com/inward/record.url?scp=10344225629&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=10344225629&partnerID=8YFLogxK

M3 - Article

VL - 178

SP - 6587

EP - 6598

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 22

ER -