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Titolo:
A unipolarly located, cell-surface-associated agglutinin, RapA, belongs toa family of Rhizobium-adhering proteins (Rap) in Rhizobium leguminosarum bv. trifolii
Autore:
Ausmees, N; Jacobsson, K; Lindberg, M;
Indirizzi:
Swedish Univ Agr Sci, Dept Microbiol, SLU, S-75007 Uppsala, Sweden SwedishUniv Agr Sci Uppsala Sweden S-75007 SLU, S-75007 Uppsala, Sweden
Titolo Testata:
MICROBIOLOGY-UK
, volume: 147, anno: 2001,
parte:, 3
pagine: 549 - 559
SICI:
1350-0872(200103)147:<549:AULCAR>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
ROOT HAIR TIPS; CARBOHYDRATE-BINDING ACTIVITIES; BRADYRHIZOBIUM-JAPONICUM; CA-2+-DEPENDENT ADHESIN; PHAGE DISPLAY; BIOVAR VICIAE; 1ST STEP; LECTIN; ATTACHMENT; RECEPTORS;
Keywords:
rhizobia; lectin; calcium-binding protein; phage display;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Ausmees, N Swedish Univ Agr Sci, Dept Microbiol, SLU, Box 7025, S-75007 Uppsala, Sweden Swedish Univ Agr Sci Box 7025 Uppsala Sweden S-75007 a, Sweden
Citazione:
N. Ausmees et al., "A unipolarly located, cell-surface-associated agglutinin, RapA, belongs toa family of Rhizobium-adhering proteins (Rap) in Rhizobium leguminosarum bv. trifolii", MICROBIO-UK, 147, 2001, pp. 549-559

Abstract

The phage-display cloning technique was used to find rhizobial proteins that bind to receptors located on the bacterial cell surface. The aim was to clone the gene(s) encoding rhicadhesin, a universal rhizobial adhesion protein, and/or other cell-surface-binding proteins. Four such Rhizobium-adhering proteins (Rap) were revealed in Rhizobium leguminosarum by. trifolii strain R200. The binding is mediated by homologous Ra domains in these proteins. One member of the Rap protein family, named RapA1, is a secreted calcium-binding protein, which are also properties expected for rhicadhesin. However, the size of the protein (24 kDa instead of 14 kDa) and its distributionamong different rhizobia (present in only Rhizobium leguminosarum biovars and R. etli instead of all members of Rhizobiaceae) argue against RapA1 being rhicadhesin. Protein RapA1 consists of two homologous Pa domains and agglutinates R200 cells by binding to specific receptors located at one cell pole during exponential growth. Expression of these cell-surface receptors was detected only in rhizobia that produce the RapA proteins. The authors propose that the homologous Pa domains, found to be present also in other proteins with different structure, represent lectin domains, which confer uponthese proteins the ability to recognize their cognate carbohydrate structures.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 01:55:37