Unusually high conservation of untranslated sequences in cDNAs for Trimeresurus flavoviridis phospholipase A2 isozymes

T. Ogawa, N. Oda, K. I. Nakashima, H. Sasaki, Masahira Hattori, Y. Sakaki, H. Kihara, M. Ohno

Research output: Contribution to journalArticle

96 Citations (Scopus)

Abstract

As a step toward understanding the structure and function of phospholipases A2 (PLA2s), we isolated and sequenced several cDNAs encoding Trimeresurus flavoviridis venom PLA2 isozymes including two [Lys49]PLA2s called basic proteins I and II, [Thr37]PLA2, and PLX'-PLA2. Comparison of the nucleotide sequences of these cDNAs with the previously isolated [Asp49]PLA2 cDNA revealed some interesting findings from the viewpoint of evolution. First, the homologies of the 5' and 3' untranslated regions (98% and 89%, respectively) were much higher than that of the protein-coding regions (67%). The predicted secondary structure showed the characteristic stemloop structures for both the untranslated regions of the mRNAs, suggesting that these regions play some functional role(s) in translation or stability of mRNAs. Second, base substitutions appeared to have occurred at similar rates for the three positions of codons among these PLA2s. The results are discussed in terms of evolution of PLA2s. Northern blot analysis showed that these PLA2s are specific to venom gland.

Original languageEnglish
Pages (from-to)8557-8561
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number18
Publication statusPublished - 1992
Externally publishedYes

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Trimeresurus
Phospholipases A2
Isoenzymes
Complementary DNA
Group II Phospholipases A2
Untranslated Regions
5' Untranslated Regions
RNA Stability
Venoms
3' Untranslated Regions
Codon
Northern Blotting
Open Reading Frames
Messenger RNA

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Unusually high conservation of untranslated sequences in cDNAs for Trimeresurus flavoviridis phospholipase A2 isozymes. / Ogawa, T.; Oda, N.; Nakashima, K. I.; Sasaki, H.; Hattori, Masahira; Sakaki, Y.; Kihara, H.; Ohno, M.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, No. 18, 1992, p. 8557-8561.

Research output: Contribution to journalArticle

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AU - Oda, N.

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AU - Hattori, Masahira

AU - Sakaki, Y.

AU - Kihara, H.

AU - Ohno, M.

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AB - As a step toward understanding the structure and function of phospholipases A2 (PLA2s), we isolated and sequenced several cDNAs encoding Trimeresurus flavoviridis venom PLA2 isozymes including two [Lys49]PLA2s called basic proteins I and II, [Thr37]PLA2, and PLX'-PLA2. Comparison of the nucleotide sequences of these cDNAs with the previously isolated [Asp49]PLA2 cDNA revealed some interesting findings from the viewpoint of evolution. First, the homologies of the 5' and 3' untranslated regions (98% and 89%, respectively) were much higher than that of the protein-coding regions (67%). The predicted secondary structure showed the characteristic stemloop structures for both the untranslated regions of the mRNAs, suggesting that these regions play some functional role(s) in translation or stability of mRNAs. Second, base substitutions appeared to have occurred at similar rates for the three positions of codons among these PLA2s. The results are discussed in terms of evolution of PLA2s. Northern blot analysis showed that these PLA2s are specific to venom gland.

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