Cell wall proteins of Aquaspirillum serpens.

AUTOR(ES)

Koval, S F

RESUMO

The Triton X-100-insoluble wall fraction of Aquaspirillum serpens VHA contained three major proteins: the regularly structured (RS) superficial protein (molecular weight 140,000) and two peptidoglycan-associated proteins (molecular weights, 32,000 and 33,000). The molecular arrangement and interactions of the outer membrane and RS proteins were examined with the use of bifunctional cross-linking reagents. The peptidoglycan-associated and RS proteins were not readily cross-linked in either homo- or heteropolymers. This suggests that the free amino groups are not suitably disposed for cross-linking. Some high-molecular-weight multimers of the RS protein were produced, but the subunit structure of the RS array was not stabilized by cross-linking. The peptidoglycan-associated proteins were cross-linked to high-molecular-weight multimers, but no dimers or trimers were produced. This result suggests that these proteins exist in the outer membrane as multimers larger than trimers.

Documentos Relacionados

• Analysis of the cell wall and lipopolysaccharide of Spirillum serpens.
• Cell envelope associations of Aquaspirillum serpens flagella.
• Substructure and in vitro assembly of the outer, structured layer of Spirillum serpens.
• Structure of the regular surface layer of Aquaspirillum serpens MW5.
• Defined medium for Aquaspirillum serpens VHL effective in batch and continuous culture.