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РЖ ВИНИТИ 34 (BI49) 96.01-04Я6.310

Membrane topology and assembly of the outer membrane protein OmpA of Escherichia coli K12 [Text] / Georg Ried [et al.] // Mol. and Gen. Genet. - 1994. - Vol. 243, N 2. - P127-135 . - ISSN 0026-8925
Перевод заглавия: Мембранная топология и организация белка внешней мембраны OmpA из Escherichia coli K12
Аннотация: The 325-residue outer membrane protein OmpA of Escherichia coli has been proposed to consist of a membrane-embedded moiety (residues 1 to about 170) and a C-terminal periplasmic region. The former is thought ot comprise eight transmembrane segments in the form of antiparallel 'бета'-strands, forming an amphiphilic 'бета'-barrel, connected by exposed turns. Several questions concerning this model were addressed. Thus no experimental evidence had been presented for the turns at the inner leaflet of the membrane and it was not known whether or not the periplasmic part of the polypeptide plays a role in the process of membrane incorporation. Oligonucleotides encoding trypsin cleavage sites were inserted at the predicted turn sites of the ompA gene and it was shown that the encoded proteins indeed become accessible to trypsin at the modified sites. Together with previous results, these data also show that the turns on both sides of the membrane do not prossess specifically topogenic information. In two cases one of the two expected tryptic fragments was lost and could be detected at low concentration in only one case. Therefore, bilateral proteolytic digestion of outer membranes can cause loss of 'бета'-strands and does not necessarily produce a reliable picture of protein topology. When ompA genes were constructed coding for proteins ending at residue 228 or 274, the membrane assembly of these proteins was shown to be partially defective with about 20% of the proteins not being assembled. No such defect was observed when, following the introduction of a premature stop codon, a truncated protein was produced ending with residue 171. It is concluded that (1) the proposed 'бета'-barrel structure is essentially correct and (2) the periplasmic part of OmpA does not play an active role in, but can, when present in mutant form, interfere with membrane assembly. Германия, Max-Planck-Inst. Biol., Correnstr. 38, D-72076 Tubingen. Библ. 46

ГРНТИ	34.19.25

ВИНИТИ 341.19.25.07
Рубрики: БЕЛОК
ВНЕШНЕЙ МЕМБРАНЫ OMPA
ОРГАНИЗАЦИЯ
ТОПОЛОГИЯ
МЕМБРАНЫ БАКТЕРИАЛЬНЫЕ
E. COLI

Доп.точки доступа:
Ried, Georg; Koebnik, Ralf; Hindennach, Ingrid; Mutscler, Bettina; Henning, Ulf

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