Vinod K. Kannaujiya

GC constituents and relative codon expressed amino acid composition in cyanobacterial phycobiliproteins

The genomic as well as structural relationship of phycobiliproteins (PBPs) in different cyanobacterial species are determined by nucleotides as well as amino acid composition. The genomic GC constituents influence the amino acid variability and codon usage of particular subunit of PBPs. We have analyzed 11 cyanobacterial species to explore the variation of amino acids and causal relationship between GC constituents and codon usage. The study at the first, second and third levels of GC content showed relatively more amino acid variability on the levels of G3+C3 position in comparison to the first and second positions. The amino acid encoded GC rich level including G rich and C rich or both correlate the codon variability and amino acid availability. The fluctuation in amino acids such as Arg, Ala, His, Asp, Gly, Leu and Glu in α and β subunits was observed at G1C1 position; however, fluctuation in other amino acids such as Ser, Thr, Cys and Trp was observed at G2C2 position. The coding selection pressure of amino acids such as Ala, Thr, Tyr, Asp, Gly, Ile, Leu, Asn, and Ser in α and β subunits of PBPs was more elaborated at G3C3 position. In this study, we observed that each subunit of PBPs is codon specific for particular amino acid. These results suggest that genomic constraint linked with GC constituents selects the codon for particular amino acids and furthermore, the codon level study may be a novel approach to explore many problems associated with genomics and proteomics of cyanobacteria.

Peroxide scavenging potential of ultraviolet-B-absorbing mycosporine-like amino acids isolated from a marine red alga Bryocladia sp.

Ultraviolet-B (UV-B; 280-315 nm)-absorbing mycosporine-like amino acids (MAAs) were extracted and purified from a marine red alga Bryocladia sp. by using high performance liquid chromatography. We have detected four MAAs having retention times 3.23, 2.94, 3.56 and 2.67 min with absorbance maxima (λmax) at 323, 328, 335 and 340 nm respectively. The effect of UV-B on the induction of these MAAs was studied. In comparison to control, there was 3 - 22 % induction of MAAs after 12 and 24 h of UV-B exposure. Apart from MAAs, other pigments such as chl a, carotenoids and total proteins were inversely affected by UV-B irradiation. In addition, peroxide scavenging potential of these MAAs were also investigated. With 2 mM hydrogen peroxide (H2O2) concentration, only <5 % of MAAs were found to be affected. However, with the increased H2O2, 40-60 % decline in the MAAs concentration with a corresponding peak shifting towards the blue wavelength was recorded. In addition, most of the MAAs were found to be reacting slowly with increasing H2O2 (upto 10 mM) concentration after an incubation period of 5 and 30 min, which indicates the remarkable scavenging potential and stability of MAAs against oxidative stress. Thus, the isolated MAAs from marine red alga Bryocladia sp. may act as an efficient peroxide scavenger.

Codon usage analysis of photolyase encoding genes of cyanobacteria inhabiting diverse habitats

Abstract Nucleotide and amino acid compositions were studied to determine the genomic and structural relationship of photolyase gene in freshwater, marine and hot spring cyanobacteria. Among three habitats, photolyase encoding genes from hot spring cyanobacteria were found to have highest GC content. The genomic GC content was found to influence the codon usage and amino acid variability in photolyases. The third position of codon was found to have more effect on amino acid variability in photolyases than the first and second positions of codon. The variation of amino acids Ala, Asp, Glu, Gly, His, Leu, Pro, Gln, Arg and Val in photolyases of three different habitats was found to be controlled by first position of codon (G1C1). However, second position (G2C2) of codon regulates variation of Ala, Cys, Gly, Pro, Arg, Ser, Thr and Tyr contents in photolyases. Third position (G3C3) of codon controls incorporation of amino acids such as Ala, Phe, Gly, Leu, Gln, Pro, Arg, Ser, Thr and Tyr in photolyases from three habitats. Photolyase encoding genes of hot spring cyanobacteria have 85% codons with G or C at third position, whereas marine and freshwater cyanobacteria showed 82 and 60% codons, respectively, with G or C at third position. Principal component analysis (PCA) showed that GC content has a profound effect in separating the genes along the first major axis according to their RSCU (relative synonymous codon usage) values, and neutrality analysis indicated that mutational pressure has resulted in codon bias in photolyase genes of cyanobacteria.