Porin and porin-associated protein (PAP) of Rhodospirillum rubrum FR1

U. Neumann; R. Benz; J. P. Rosenbusch; B. Stahl; J. Weckesser

doi:10.1099/13500872-141-12-3155

Porin and porin-associated protein (PAP) of Rhodospirillum rubrum FR1

U. Neumann, R. Benz, J. P. Rosenbusch, B. Stahl, J. Weckesser^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

The porin of Rhodospirillum rubrum FR1 was found in the outer membrane as a complex with a relatively small (32 kDa) porin-associated protein (PAP). The porin moiety of the complex consisted of a trimer which revealed a mainly β-sheet structure, while the porin-PAP complex also contained a significant α-helical portion. Isolated PAP exhibited a mostly α-helical structure. The porin-PAP complex had the same single-channel conductivity (2.8 nS) as the isolated porin, demonstrating that PAP did not affect the porin channel size. Differential extraction of the cell wall fraction with N,N-dimethyldodecylamine N-oxide revealed that PAP stabilized the porin in the outer membrane. EDTA caused dissociation of the porin-PAP complex, indicating that divalent cations were involved in formation of this complex.

Original language	English
Pages (from-to)	3155-3160
Number of pages	6
Journal	Microbiology
Volume	141
Issue number	12
DOIs	https://doi.org/10.1099/13500872-141-12-3155
Publication status	Published - 1995
Externally published	Yes

Keywords

Membrane protein
Outer membrane
Porin
Porin-associated protein (PAP)
Rhodospirillum rubrum

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10.1099/13500872-141-12-3155

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title = "Porin and porin-associated protein (PAP) of Rhodospirillum rubrum FR1",

abstract = "The porin of Rhodospirillum rubrum FR1 was found in the outer membrane as a complex with a relatively small (32 kDa) porin-associated protein (PAP). The porin moiety of the complex consisted of a trimer which revealed a mainly β-sheet structure, while the porin-PAP complex also contained a significant α-helical portion. Isolated PAP exhibited a mostly α-helical structure. The porin-PAP complex had the same single-channel conductivity (2.8 nS) as the isolated porin, demonstrating that PAP did not affect the porin channel size. Differential extraction of the cell wall fraction with N,N-dimethyldodecylamine N-oxide revealed that PAP stabilized the porin in the outer membrane. EDTA caused dissociation of the porin-PAP complex, indicating that divalent cations were involved in formation of this complex.",

keywords = "Membrane protein, Outer membrane, Porin, Porin-associated protein (PAP), Rhodospirillum rubrum",

author = "U. Neumann and R. Benz and Rosenbusch, {J. P.} and B. Stahl and J. Weckesser",

year = "1995",

doi = "10.1099/13500872-141-12-3155",

language = "English",

volume = "141",

pages = "3155--3160",

journal = "Microbiology",

issn = "1350-0872",

publisher = "Microbiology Society",

number = "12",

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TY - JOUR

T1 - Porin and porin-associated protein (PAP) of Rhodospirillum rubrum FR1

AU - Neumann, U.

AU - Benz, R.

AU - Rosenbusch, J. P.

AU - Stahl, B.

AU - Weckesser, J.

PY - 1995

Y1 - 1995

N2 - The porin of Rhodospirillum rubrum FR1 was found in the outer membrane as a complex with a relatively small (32 kDa) porin-associated protein (PAP). The porin moiety of the complex consisted of a trimer which revealed a mainly β-sheet structure, while the porin-PAP complex also contained a significant α-helical portion. Isolated PAP exhibited a mostly α-helical structure. The porin-PAP complex had the same single-channel conductivity (2.8 nS) as the isolated porin, demonstrating that PAP did not affect the porin channel size. Differential extraction of the cell wall fraction with N,N-dimethyldodecylamine N-oxide revealed that PAP stabilized the porin in the outer membrane. EDTA caused dissociation of the porin-PAP complex, indicating that divalent cations were involved in formation of this complex.

AB - The porin of Rhodospirillum rubrum FR1 was found in the outer membrane as a complex with a relatively small (32 kDa) porin-associated protein (PAP). The porin moiety of the complex consisted of a trimer which revealed a mainly β-sheet structure, while the porin-PAP complex also contained a significant α-helical portion. Isolated PAP exhibited a mostly α-helical structure. The porin-PAP complex had the same single-channel conductivity (2.8 nS) as the isolated porin, demonstrating that PAP did not affect the porin channel size. Differential extraction of the cell wall fraction with N,N-dimethyldodecylamine N-oxide revealed that PAP stabilized the porin in the outer membrane. EDTA caused dissociation of the porin-PAP complex, indicating that divalent cations were involved in formation of this complex.

KW - Membrane protein

KW - Outer membrane

KW - Porin

KW - Porin-associated protein (PAP)

KW - Rhodospirillum rubrum

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U2 - 10.1099/13500872-141-12-3155

DO - 10.1099/13500872-141-12-3155

M3 - Article

AN - SCOPUS:0029566034

SN - 1350-0872

VL - 141

SP - 3155

EP - 3160

JO - Microbiology

JF - Microbiology

IS - 12

ER -

Porin and porin-associated protein (PAP) of Rhodospirillum rubrum FR1

Abstract

Keywords

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