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Gene Review

SNL1  -  Snl1p

Saccharomyces cerevisiae S288c

Synonyms: HSP70 co-chaperone SNL1, Suppressor of NUP116-C lethal, YIL016W
 
 
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High impact information on SNL1

  • In live yeast, mutated Snl1p could not substitute for wild-type Snl1p in suppressing the lethal defect caused by truncation of the Nup116p nuclear pore component [1].
  • Point mutations in Snl1p that disrupted the conserved residues Glu-112 and Arg-141, equivalent to Glu-212 and Arg-237 in Bag-1M, abolished the interaction with Hsp70 proteins [1].
  • Thus, Snl1p is the first Bag domain protein identified in S. cerevisiae, and its interaction with Hsp70 is essential for biological activity [1].
  • Snl1p has a predicted molecular mass of 18.3 kDa, a putative transmembrane domain, and limited sequence similarity to Pom152p, the only previously identified yeast NPC-associated integral membrane protein [2].
  • The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function [2].
 

Anatomical context of SNL1

References

  1. Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. Sondermann, H., Ho, A.K., Listenberger, L.L., Siegers, K., Moarefi, I., Wente, S.R., Hartl, F.U., Young, J.C. J. Biol. Chem. (2002) [Pubmed]
  2. The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function. Ho, A.K., Raczniak, G.A., Ives, E.B., Wente, S.R. Mol. Biol. Cell (1998) [Pubmed]
 
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