"Partial molecular characterization of putative lysophosphatidic acid a" by May Anne O. Argayoso

Partial molecular characterization of putative lysophosphatidic acid acyl transferase gene cloned from coconut (Cocos nucifera L.) endosperm.

Date

4-2005

Degree

Bachelor of Science in Biology

College

College of Arts and Sciences (CAS)

Adviser/Committee Chair

Genaleen Q. Diaz

Co-adviser

Marni E. Cueno

Abstract

Lysophosphatidic acid acyl transferase (LPAAT) gene from a 6-month old coconut endosperm was isolated and cloned using the TOPO® TA cloning technique and was sent to Korea (MACROGEN) for sequencing. The sequence obtained consisted of 928 bp. However, sequence analysis showed a chimeric pattern. Using the BLASTX program, the sequence found prior to the primer and the putative LPAAT gene were identified and analyzed. The sequence prior to the primer showed highest hit on LacOPZ-alpha peptide from Cryptosporidium hominis and the other were vector sequences indicating that it was derived from the vector. The sequence from the primer to the last base obtained two out of six matches with other LPAAT sequences. One of the matches was with LPAAT yeast wherein from the 33 amino acids that have aligned, only 14 have matched. These matches are 36% identical and 42% similar. The matches with LPAAT mouse also produced alignment wherein 8 out of 13 amino acids have matched. These matches are 58% identical and 66% similar. Homology among different LPAAT genes from the database suggested that a putative LPAAT gene from a coconut endosperm might have been cloned. Further observation in the sequence revealed the presence of specific cleavage and ligation recognized by the topoisomerase which might have eventually led to the formation of the observed chimeric sequences.

Language

English

Location

UPLB Main Library Special Collections Section (USCS)

Call Number

Thesis

Document Type

Thesis

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