Add time:07/30/2019         Source:sciencedirect.com

We have determined the nucleotide (nt) and deduced amino acid (aa) sequences of a unique 1115-kDa. Mycoplasma hyorhinis protein (P 115) with an N-terminal region containing a highly conserved consensus sequence characteristic of nt-binding domains of several ATPase and GTPase enzymes. However, PI 15 lacked additional conserved features characteristic of some classes of nt-binding proteins. Based on the hydropathy profile of the deduced aa sequence, the absence of a leader peptide, its exclusive partitioning into the hydrophilic phase during Triton X-114 phase fractionation of M. hyorhinis, and immunofluorescence analysis indicating no surface-exposed domains, it was concluded that P 115 is a cytoplasmic protein lacking intrinsic membrane interaction. M. hyorhinis P 115 appears to be a species-specific protein, since it was not detected in any other mycoplasmal or bacterial species examined with specific antibody or genomic probes. Since genetic systems for direct mutational analysis are currently unavailable in this organism, sequence analysis provides critical information in establishing the possible function of this protein. Moreover, the nt sequence encoding PI 15 reported here supports a previously proposed model, based on synthesis of P115-related proteins in Escherichia coli, suggesting that multiple polypeptide products can be generated from mycoplasma genes by promiscuous translation initiation in this heterologous expression system.

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