The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli.
The free and bound forms of Lpp occupy distinct subcellular locations in Escherichia coli.
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DOI:
10.1111/j.1365-2958.2011.07539.x
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发表时间:
2011-03
影响因子:
3.6
通讯作者:
Silhavy TJ
中科院分区:
文献类型:
--
作者:
Cowles CE;Li Y;Semmelhack MF;Cristea IM;Silhavy TJ
The lipoprotein Lpp is the most numerically abundant protein in Escherichia coli, has been investigated for over 40 years, and has served as the paradigmatic bacterial lipoprotein since its initial discovery. It exists in two distinct forms: a “bound-form”, which is covalently bound to the cell’s peptidoglycan layer, and a “free-form”, which is not. Although it is known that the carboxyl-terminus of bound-form Lpp is located in the periplasm, the precise location of free-form Lpp has never been determined. For decades, it has been widely assumed that free-form Lpp is associated with bound-form. In this work, we show that the free and bound forms of Lpp are not largely associated with each other, but are found in distinct subcellular locations. Our results indicate that free-form Lpp spans the outer membrane and is surface-exposed, whereas bound-form Lpp resides in the periplasm. Thus, Lpp represents a novel example of a single lipoprotein that is able to occupy distinct subcellular locations, and challenges models in which the free and bound forms of Lpp are assumed to be associated with each other.
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DOI:
10.1016/j.jasms.2009.08.026
发表时间:
2010-01
影响因子:
3.2
作者:
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通讯作者:
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DOI:
10.1073/pnas.77.8.4592
发表时间:
1980-01-01
期刊:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES
影响因子:
--
作者:
CHEN, R;SCHMIDMAYR, W;HENNING, U
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HENNING, U
影响因子:
3.2
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COLE, ST;CHENSCHMEISSER, U;HENNING, U
通讯作者:
HENNING, U
影响因子:
3.6
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通讯作者:
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DOI:
10.1111/j.1432-1033.1970.tb00936.x
发表时间:
1970-01-01
期刊:
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子:
--
作者:
BRAUN, V;SIEGLIN, U
通讯作者:
SIEGLIN, U