Primary structure and glycosylation of the S-layer protein of Haloferax volcanii.

摘要: The outer surface of the archaebacterium Haloferax volcanii (formerly named Halobacterium volcanii) is covered with a hexagonally packed (S) layer. gene coding for S-layer protein was cloned and sequenced. mature polypeptide composed 794 amino acids preceded by typical signal sequence 34 acid residues. A highly hydrophobic stretch 20 at C-terminal end probably serves as transmembrane domain. Clusters threonine residues are located adjacent to this membrane anchor. glycoprotein containing both N- O-glycosidic bonds. Glucosyl-(1----2)-galactose disaccharides linked primary structure glycosylation pattern glycoproteins from halobium were compared found exhibit distinct differences, despite fact that three-dimensional reconstructions electron micrographs revealed no structural differences least 2.5-nm level attained so far (M. Kessel, I. Wildhaber, S. Cohe, W. Baumeister, EMBO J. 7:1549-1554, 1988).