Mutagenesis of conserved charged amino acids in SLH domains of Thermoanaerobacterium thermosulfurigenes EM1 affects attachment to cell wall sacculi
- Author
- MAY, Antje1 ; PUSZTAHELYI, Tünde1 ; HOFFMANN, Nadine1 ; FISCHER, Ralf-Jörg1 ; BAHL, Hubert1
[1] Institute of Biological Sciences, Division of Microbiology, University of Rostock, Albert-Einstein-Str. 3, 18051 Rostock, Germany - Source
Archives of microbiology. 2006, Vol 185, Num 4, pp 263-269, 7 p ; ref : 35 ref
- CODEN
- AMICCW
- ISSN
- 0302-8933
- Scientific domain
- Biotechnology; Microbiology, infectious diseases
- Publisher
- Springer, Berlin
/
Springer, Heidelberg
- Publication country
- Germany
- Document type
- Article
- Language
- English
- Author keyword
- Cell wall polymer Extracellular enzymes Gram-positive S-layer (surface layer) homologous domain S-layer protein
- Keyword (fr)
- Bactérie Gram positif Bactérie Couche S Enzyme Mutagenèse Paroi cellulaire Protéine Relation structure propriété Surface cellulaire Thermoanaerobacterium thermosulfurigenes
- Keyword (en)
- Gram positive bacteria Bacteria S Layer Enzyme Mutagenesis Cell wall Protein Property structure relationship Cell surface
- Keyword (es)
- Bacteria Gram positiva Bacteria Capa S Enzima Mutagénesis Pared celular Proteína Relación estructura propiedad Superficie celular
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A05 Microbiology / 002A05B Bacteriology / 002A05B03 Morphology, structure, chemical composition
- Discipline
- Microbiology
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 17755289
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.1007/s00203-006-0092-x 
https://dx.doi.org/10.1007/s00203-006-0092-x
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