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Gene Review

nas-30  -  Protein NAS-30

Caenorhabditis elegans

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High impact information on peptidase

  • We have discovered roles for the C. elegans puromycin-sensitive aminopeptidase PAM-1 in both cell cycle progression and AP axis formation, further implicating proteolytic regulation in these processes. pam-1 mutant embryos exhibit a delay in exit from meiosis: thus, this peptidase is required for progression to mitotic interphase [1].
  • The predicted amino acid sequence of the putative extracellular form contained an N-terminal extension with the characteristics of a signal sequence including a potential signal peptidase cleavage site [2].
  • This deduced structure of the enzyme revealed a multi-domain protein that included an NH2-terminal peptidase [3].
  • This peptidase consisted of a signal peptide, a pro-enzyme region, and a mature peptidase domain that included the metal ion co-ordinating motifs, HETSHALGVIH and SIMHY ("Met-turn"), characteristic of the catalytic active site of members of the metzincin superfamily of zinc metallo-endopeptidases [3].


  1. The puromycin-sensitive aminopeptidase PAM-1 is required for meiotic exit and anteroposterior polarity in the one-cell Caenorhabditis elegans embryo. Lyczak, R., Zweier, L., Group, T., Murrow, M.A., Snyder, C., Kulovitz, L., Beatty, A., Smith, K., Bowerman, B. Development (2006) [Pubmed]
  2. Extracellular and cytoplasmic Cu/Zn superoxide dismutases from Haemonchus contortus. Liddell, S., Knox, D.P. Parasitology (1998) [Pubmed]
  3. Identification of an astacin-like metallo-proteinase transcript from the infective larvae of Strongyloides stercoralis. Gomez Gallego, S., Loukas, A., Slade, R.W., Neva, F.A., Varatharajalu, R., Nutman, T.B., Brindley, P.J. Parasitol. Int. (2005) [Pubmed]
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