Date of Award


Document Type


Degree Name

Master of Science (MS)


College of Science and Mathematics



Thesis Sponsor/Dissertation Chair/Project Chair

John Gaynor

Committee Member

Paul Bologna

Committee Member

Charles Du


The scyphozoan jellyfish Chrysaora quinquecirrha (CQ) is becoming a major pest of Eastern bays and waterways due to changing environmental conditions, including the warming of inlet waters, man-made plastic bulkheads and reduced plant life which serve as havens for their predators. Their increasing numbers warrants investigations into population control of these animals. Therefore any information about them may help in understanding and eventually controlling jellyfish blooms.

ß-actin is a ubiquitous cytoskeletal protein that has many essential functions. The protein and nucleotide sequences are highly conserved across all species, yet the number, size and sequences of the introns are highly variable. This makes ß-actin an interesting protein to study across many species in order to discover phylogenetic relationships.

A partial (86%) nucleotide and amino acid sequence of the ß-actin gene from CQ genomic DNA has been identified and compared to a broad selection of species, including other cnidarians. It was found that this partial p-actin sequence from CQ is 98% identical to the box jellyfish Malo kingi, and 95% identical to the human form at the protein level. However, the nucleotide sequence is 84% identical for M. kingi while only 78% identical for human. The 2 introns in the CQ sequence are found at the same locations in Podocoryne carnea, a colonial Hydrozoan. A BLAST to the 60 amino acid ß-actin sequence from C. colorata shows 6 amino acid differences, a surprisingly high number in such a short segment. Further work to sequence the 5’ and 3’ ends, including UTRs, should bring to light further interesting aspects of ß-actin, since these regions are involved in mRNA and protein regulation.

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Biology Commons