Unknown

Dataset Information

0

Isolation and characterization of a cDNA clone encoding an alternative oxidase protein of Sauromatum guttatum (Schott).


ABSTRACT: Polyclonal and monoclonal antibodies that recognize the 35-, 36-, and 37-kDa alternative oxidase proteins of Sauromatum guttatum (Schott) were used to isolate a cDNA clone, pAOSG81, from an S. guttatum cDNA expression library. A fusion protein with an apparent molecular mass of 48 kDa was expressed from a pUC119 derivative of pAOSG81 (pAOSG81-119) in Escherichia coli cells and was recognized by the monoclonal antibodies. When the in vitro translated and immunoprecipitated products made from mRNA hybrid-selected by pAOSG81 were analyzed, a single band corresponding to a protein with an apparent molecular mass of 42 kDa was observed. DNA sequence characterization showed that pAOSG81 contains the entire coding region of a protein with a calculated molecular mass of 38.9 kDa, a putative 63-amino acid transit peptide, and a 9-amino acid match to the authentic N-terminal sequence of the 36-kDa alternative oxidase protein. Analyses of the deduced amino acid sequence indicate: (i) that the transit peptide is predicted to form amphiphilic helices, and (ii) that three regions of the processed protein are likely to form transmembrane alpha-helices. We conclude from these data that pAOSG81 represents a nuclear gene, aox1, encoding a precursor protein of one or more of the alternative oxidase proteins of S. guttatum.

SUBMITTER: Rhoads DM 

PROVIDER: S-EPMC51181 | biostudies-other | 1991 Mar

REPOSITORIES: biostudies-other

altmetric image

Publications

Isolation and characterization of a cDNA clone encoding an alternative oxidase protein of Sauromatum guttatum (Schott).

Rhoads D M DM   McIntosh L L  

Proceedings of the National Academy of Sciences of the United States of America 19910301 6


Polyclonal and monoclonal antibodies that recognize the 35-, 36-, and 37-kDa alternative oxidase proteins of Sauromatum guttatum (Schott) were used to isolate a cDNA clone, pAOSG81, from an S. guttatum cDNA expression library. A fusion protein with an apparent molecular mass of 48 kDa was expressed from a pUC119 derivative of pAOSG81 (pAOSG81-119) in Escherichia coli cells and was recognized by the monoclonal antibodies. When the in vitro translated and immunoprecipitated products made from mRNA  ...[more]

Similar Datasets

| S-EPMC7172579 | biostudies-literature
| S-EPMC53330 | biostudies-other
| S-EPMC286480 | biostudies-other
| S-EPMC312894 | biostudies-literature
| S-EPMC53645 | biostudies-other
| S-EPMC2803416 | biostudies-literature
| S-EPMC1151258 | biostudies-other
| S-EPMC2721051 | biostudies-literature
| S-EPMC3901258 | biostudies-literature
| S-EPMC55121 | biostudies-other