An anaerobic protein (ANP) that may not be a glycolytic enzyme

--Wolfgang Kammerer and Michael Freeling

Anaerobiosis induces the expression of a specific set of genes yielding a highly changed pattern of protein biosynthesis. The expression of these newly synthesized anaerobic proteins (ANP's) is regulated at the transcriptional as well as the posttranscriptional level (Sachs, Freeling and Okimoto, Cell 20:761, 1980 ). Work done in this and other labs has shown that the ANPs are glycolytic enzymes (Bailey-Serres et al., Plant, Cell and Environment 11:351, 1988). We report here progress in the study of a 31kD protein, which is one of the prominent ANPs and is rapidly induced as mRNA and protein after the onset of anaerobiosis (ANP31; Hake et al., JBC 260:5050, 1985 ). We have isolated an apparently full length cDNA clone and sequenced it in order to get a clue about the function of the protein product. The full length clone was isolated by D.C. Bennett from a cDNA library prepared by P. Kelley (unpublished) using the Hake cDNA probe (this laboratory). According to the sequence, the protein is 29.8kD in size, has a 119bp untranslated 5' leader region as well as 191bp untranslated sequence at the 3' end, containing two possible polyadenylation signals; the second one is located about 20bp upstream of the polyA sequence.

Sequence comparison using the EMBL/Genbank database revealed no good similarities with any of the available sequences, including glycolytic enzymes. There was only weak similarity with some viral proteins and protamines, which is most likely caused by the unusually high content of the positively charged amino acid arginine (19%). Another quite unusual feature is the very high G+C content of the gene, which is about 75% overall and about 85% in the middle third. We are currently trying to express this protein in order to raise antibodies, etc. While most ANPs are certainly glycolytic enzymes, perhaps this one has a binding function.

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