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Titolo:
Plant virus transmission by plasmodiophorid fungi is associated with distinctive transmembrane regions of virus-encoded proteins
Autore:
Adams, MJ; Antoniw, JF; Mullins, JGL;
Indirizzi:
IACR Rothamsted, Dept Plant Pathol, Harpenden AL5 2JQ, Herts, England IACRRothamsted Harpenden Herts England AL5 2JQ n AL5 2JQ, Herts, England IACR Rothamsted, Bioinformat Dept, Harpenden AL5 2JQ, Herts, England IACR Rothamsted Harpenden Herts England AL5 2JQ n AL5 2JQ, Herts, England Univ Luton, Dept Biol & Hlth Sci, Luton, Beds, England Univ Luton Luton Beds England Dept Biol & Hlth Sci, Luton, Beds, England
Titolo Testata:
ARCHIVES OF VIROLOGY
fascicolo: 6, volume: 146, anno: 2001,
pagine: 1139 - 1153
SICI:
0304-8608(2001)146:6<1139:PVTBPF>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
WHEAT MOSAIC-VIRUS; COMPLETE NUCLEOTIDE-SEQUENCE; TRANSMITTED UK ISOLATE; MOP-TOP VIRUS; READTHROUGH PROTEIN; GENETIC ORGANIZATION; STRUCTURE PREDICTION; POLYMYXA-BETAE; COAT PROTEIN; BEET;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
Recensione:
Indirizzi per estratti:
Indirizzo: Adams, MJ IACR Rothamsted, Dept Plant Pathol, Harpenden AL5 2JQ, Herts, England IACR Rothamsted Harpenden Herts England AL5 2JQ Herts, England
Citazione:
M.J. Adams et al., "Plant virus transmission by plasmodiophorid fungi is associated with distinctive transmembrane regions of virus-encoded proteins", ARCH VIROL, 146(6), 2001, pp. 1139-1153

Abstract

Computer analysis of published sequence data has consistently identified two complementary transmembrane domains in the coat protein readthrough domains of benyviruses, furoviruses and pomoviruses and in the P2 proteins of bymoviruses. These viruses differ in genome organisation but are all transmitted by plasmodiophorid fungi. The second domain is absent or disrupted in naturally-occurring deletion mutants that cannot be fungally-transmitted. In a non-transmissible substitution mutant of Beer necrotic yellow vein virus [Tamada et al. (1996) J Gen Virol 77: 1359-1367], the alignment of the helices is disrupted. From conserved patterns detected in transmembrane helixsequences and calculated relative helix tilts, structural arrangements consistent with tight packing of transmembrane helices were identified. These included ridge/groove arrangements between the two helices and strong electrostatic associations at the interfacial regions of the membrane. The data strongly suggest that these transmembrane helices facilitate the movement of virus particles across the fungal membrane.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 14:53:11