Literature DB >> 30729391

Myxococcus xanthus truncated globin HbO: in silico analysis and functional characterization.

Santosh Kumar Singh1, Rajinder Kaur2, Ashok Kumar3, Ramandeep Kaur4.   

Abstract

Truncated globins are 20-40 amino acids shorter than full length globins. Till date, globins have been characterized predominantly from bacteria involved in pathogenicity, nitrogen fixation and photosynthesis, where they are implicated in bacterial virulence within the host, protection of nitrogenase from oxygen inactivation and prevention of oxidative damage to the photosynthetic machinery respectively. Myxococcus xanthus, the model myxobacterium, is an obligate aerobe with a multicellular stage in its life cycle where cells encounter oxygen limitation. This work was undertaken to investigate the potential role of the truncated globin in M. xanthus. To examine the role of globins in this unique group of bacteria, the gene coding for a putative truncated globin (HbO) was identified in the genome of M. xanthus DK 1622. The sequence analysis by bioinformatics approaches revealed that HbO from M. xanthus (Mx-HbO) likely adopts a 2-on-2 alpha helical fold of the truncated globins. The gene coding for Mx-HbO was cloned and its expression in E. coli imparted reddish tinge to the cells. The spectral analysis confirmed it to be a functional globin. The expression of Mx-HbO in the heterologous host improved its growth, resulting in the attainment of higher cell density in culture. The transcript of Mx-hbO was induced threefold in the host cells when grown under low aeration condition as compared to the cells grown under high aeration condition. In M. xanthus, an obligate aerobe, where cell growth accompanies swarming, there is a higher density of cells in the middle of the swarm. Our results suggest that Mx-HbO is a functional globin and could facilitate the growth of cells facing oxygen deprivation, the condition prevailing in the middle of the swarm.

Entities:  

Keywords:  Growth advantage; Myxococcus xanthus; Transcriptional analysis; Truncated hemoglobin

Mesh:

Substances:

Year:  2019        PMID: 30729391     DOI: 10.1007/s11033-019-04662-5

Source DB:  PubMed          Journal:  Mol Biol Rep        ISSN: 0301-4851            Impact factor:   2.316


  48 in total

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Review 3.  Truncated hemoglobins: a new family of hemoglobins widely distributed in bacteria, unicellular eukaryotes, and plants.

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Journal:  J Biol Chem       Date:  2001-11-05       Impact factor: 5.157

4.  Kinetic modulation in carbonmonoxy derivatives of truncated hemoglobins: the role of distal heme pocket residues and extended apolar tunnel.

Authors:  Uri Samuni; David Dantsker; Anandhi Ray; Jonathan B Wittenberg; Beatrice A Wittenberg; Sylvia Dewilde; Luc Moens; Yannick Ouellet; Michel Guertin; Joel M Friedman
Journal:  J Biol Chem       Date:  2003-05-07       Impact factor: 5.157

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Journal:  J Bacteriol       Date:  2004-02       Impact factor: 3.490

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Journal:  J Comput Chem       Date:  2004-10       Impact factor: 3.376

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Authors:  Ranjana Pathania; Naveen K Navani; Govindan Rajamohan; Kanak L Dikshit
Journal:  J Biol Chem       Date:  2002-01-16       Impact factor: 5.157

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Authors:  R K Poole; M N Hughes
Journal:  Mol Microbiol       Date:  2000-05       Impact factor: 3.501

9.  A TyrCD1/TrpG8 hydrogen bond network and a TyrB10TyrCD1 covalent link shape the heme distal site of Mycobacterium tuberculosis hemoglobin O.

Authors:  Mario Milani; Pierre-Yves Savard; Hugues Ouellet; Paolo Ascenzi; Michel Guertin; Martino Bolognesi
Journal:  Proc Natl Acad Sci U S A       Date:  2003-04-28       Impact factor: 11.205

10.  Expression of intracellular hemoglobin improves protein synthesis in oxygen-limited Escherichia coli.

Authors:  C Khosla; J E Curtis; J DeModena; U Rinas; J E Bailey
Journal:  Biotechnology (N Y)       Date:  1990-09
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