TY  - JOUR
AB  - The structural S-layer proteins of 28 different Corynebacterium glutamicum isolates have been analyzed systematically. Treatment of whole C. glutamicum cells with detergents resulted in the isolation of S-layer proteins with different apparent molecular masses, ranging in size from 55 to 66 kDa. The S-layer genes analyzed were characterized by coding regions ranging from 1473 to 1533 nucleotides coding for S-layer proteins with a size of 490-510 amino acids. Using PCR techniques, the corresponding S-layer genes of the 28 C. glutamicum isolates were all cloned and sequenced. The deduced amino acid sequences of the S-layer proteins showed identities between 69 and 98% and could be grouped into five phylogenetic classes. Furthermore, sequence analyses indicated that the S-layer proteins of the analyzed C. glutamicum isolates exhibit a mosaic structure of highly conserved and highly variable regions. Several conserved regions were assumed to play a key role in the formation of the C. glutamicum S-layers. Especially the N-terminal signal peptides and the C-terminal anchor sequences of the S-layer proteins showed a nearly perfect amino acid sequence conservation. Analyses by atomic force microscopy revealed a committed hexagonal structure. Morphological diversity of the C. glutamicum S-layers was observed in a class-specific unit cell dimension (ranging from 15.2 to 17.4 nm), which correlates with the sequence similarity-based classification. It could be demonstrated that differences in the primary structure of the S-layer proteins were reflected by the S-layer morphology. (C) 2004 Elsevier B.V. All rights reserved.
DA  - 2004
DO  - 10.1016/j.jbiotec.2004.03.020
KW  - S-layer protein classification
KW  - Diversity
KW  - Cell envelope
KW  - Unit cell dimension
KW  - Surface-layer
KW  - Hexagonal symmetry
KW  - Corynebacterium glutamicum
LA  - eng
IS  - 1-2
M2  - 177
PY  - 2004
SN  - 0168-1656
SP  - 177-193
T2  - J Biotechnol
TI  - Classification of hyper-variable Corynebacterium glutamicum surface-layer proteins by sequence analyses and atomic force microscopy
UR  - https://nbn-resolving.org/urn:nbn:de:0070-pub-17731309
Y2  - 2024-11-22T02:57:16
ER  -