Characterization of manganese superoxide dismutase from a marine cyanobacterium Leptolyngbya valderiana BDU20041

Balakrishnan Priya, Reddi K. Sivaprasanth, Vincent D. Jensi, Lakshmanan Uma, Gopalakrishnan Subramanian, Dharmar Prabaharan

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Background: Cyanobacteria are recognized as the primordial organisms to grace the earth with molecular oxygen ~3.5 billion years ago as a result of their oxygenic photosynthesis. This laid a selection pressure for the evolution of antioxidative defense mechanisms to alleviate the toxic effect of active oxygen species (AOS) in cyanobacteria. Superoxide dismutases (SODs) are metalloenzymes that are the first arsenal in defense mechanism against oxidative stress followed by an array of antioxidative system. Unlike other living organisms, cyanobacteria possess multiple isoforms of SOD. Hence, an attempt was made to demonstrate the oxidative stress tolerance ability of marine cyanobacterium, Leptolyngbya valderiana BDU 20041 and to PCR amplify and sequence the SOD gene, the central enzyme for alleviating stress.Result: L. valderiana BDU 20041, a filamentous, non-heterocystous marine cyanobacterium showed tolerance to the tested dye (C.I. Acid Black 1) which is evident by increased in biomass (i.e.) chlorophyll a. The other noticeable change was the total ROS production by culture dosed with dye compared to the control cultures. This prolonged incubation showed sustenance, implying that cyanobacteria maintain their antioxidant levels. The third significant feature was a two-fold increase in SOD activity of dye treated L. valderiana BDU20041 suggesting the role of SOD in alleviating oxidative stress via Asada-Halliwell pathway. Hence, the organism was PCR amplified for SOD gene resulting in an amplicon of 550 bp. The sequence analysis illustrated the presence of first three residues involved in motif; active site residues at H4, 58 and D141 along with highly conserved Mn specific residues. The isolated gene shared 63.8% homology with MnSOD of bacteria confirmed it as Mn isoform. This is the hitherto report on SOD gene from marine cyanobacterium, L. valderiana BDU20041 of Indian subcontinent.Conclusion: Generation of Reactive Oxygen Species (ROS) coupled with induction of SOD by marine cyanobacterium, L. valderiana BDU20041 was responsible for alleviating stress caused by an azo dye, C. I. Acid Black 1. The partial SOD gene has been sequenced and based on the active site, motif and metal specific residues; it has been identified as Mn metalloform.

Original languageEnglish (US)
Article number6
JournalSaline Systems
Volume6
Issue number1
DOIs
StatePublished - Jun 3 2010
Externally publishedYes

Fingerprint

Leptolyngbya
Cyanobacteria
Superoxide Dismutase
manganese
cyanobacterium
superoxide dismutase
dye
gene
dyes
defense mechanism
Reactive Oxygen Species
Oxidative Stress
Coloring Agents
oxidative stress
Genes
defense mechanisms
genes
active sites
tolerance
reactive oxygen species

ASJC Scopus subject areas

  • Aquatic Science
  • Ecology, Evolution, Behavior and Systematics
  • Water Science and Technology
  • Microbiology

Cite this

Priya, B., Sivaprasanth, R. K., Jensi, V. D., Uma, L., Subramanian, G., & Prabaharan, D. (2010). Characterization of manganese superoxide dismutase from a marine cyanobacterium Leptolyngbya valderiana BDU20041. Saline Systems, 6(1), [6]. https://doi.org/10.1186/1746-1448-6-6

Characterization of manganese superoxide dismutase from a marine cyanobacterium Leptolyngbya valderiana BDU20041. / Priya, Balakrishnan; Sivaprasanth, Reddi K.; Jensi, Vincent D.; Uma, Lakshmanan; Subramanian, Gopalakrishnan; Prabaharan, Dharmar.

In: Saline Systems, Vol. 6, No. 1, 6, 03.06.2010.

Research output: Contribution to journalArticle

Priya, Balakrishnan ; Sivaprasanth, Reddi K. ; Jensi, Vincent D. ; Uma, Lakshmanan ; Subramanian, Gopalakrishnan ; Prabaharan, Dharmar. / Characterization of manganese superoxide dismutase from a marine cyanobacterium Leptolyngbya valderiana BDU20041. In: Saline Systems. 2010 ; Vol. 6, No. 1.
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AU - Prabaharan, Dharmar

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