Light-dependent regulation of the synthesis of soluble and intracytoplasmic membrane proteins of Rhodopseudomonas sphaeroides.

The accumulation of N-acylphosphatidylserine (NAPS) in response to the inclusion of Tris in the growth medium of Rhodopseudomonas sphaeroides strain M29-5 has been examined. In the accompanying paper (Donohue et al., J. Bacteriol. 152:000--000, 1982), we show that in response to Tris, NAPS accumulated to as much as 40% of the total cellular phospholipid content. NAPS accumulation began immediately upon addition of Tris and was reflected as an abrupt 12-fold increase in the apparent rate of NAPS accumulation. We suggest that Tris altered the flow of metabolites through a preexisting and previously unknown metabolic pathway. NAPS accumulation ceased immediately upon the removal of Tris; however, accumulated NAPS remained largely metabolically stable. Importantly, under conditions in which NAPS was not accumulated, the intracytoplasmic membrane was shown to be virtually devoid of newly synthesized NAPS. The significance of this observation is discussed in terms of its physiological implications on phospholipid transfer and membrane biogenesis in R. sphaeroides.

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Incorporation of Selenomethionine into Induced Intracytoplasmic Membrane Proteins of Rhodobacter species

Journal of Structural and Functional Genomics ◽

10.1007/s10969-005-1936-3 ◽

2005 ◽

Vol 6 (2-3) ◽

pp. 95-102 ◽

Cited By ~ 5

Author(s):

Philip D. Laible ◽

Aaron N. Hata ◽

Adam E. Crawford ◽

Deborah K. Hanson

Keyword(s):

Membrane Proteins ◽

Intracytoplasmic Membrane

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The relationship of intracytoplasmic membrane assembly to the cell division cycle in Rhodopseudomonas sphaeroides.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)37753-0 ◽

1979 ◽

Vol 254 (6) ◽

pp. 1980-1986 ◽

Cited By ~ 5

Author(s):

R.T. Fraley ◽

D.R. Lueking ◽

S. Kaplan

Keyword(s):

Cell Division ◽

Cell Division Cycle ◽

Rhodopseudomonas Sphaeroides ◽

Intracytoplasmic Membrane ◽

Membrane Assembly ◽

Relationship Of ◽

The Relationship

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Proteomic Characterization of the Rhodobacter sphaeroides 2.4.1 Photosynthetic Membrane: Identification of New Proteins

Journal of Bacteriology ◽

10.1128/jb.00946-07 ◽

2007 ◽

Vol 189 (20) ◽

pp. 7464-7474 ◽

Cited By ~ 27

Author(s):

Xiaohua Zeng ◽

Jung Hyeob Roh ◽

Stephen J. Callister ◽

Christine L. Tavano ◽

Timothy J. Donohue ◽

...

Keyword(s):

Membrane Proteins ◽

Rhodobacter Sphaeroides ◽

Protein Complexes ◽

Photosynthetic Apparatus ◽

Energy Utilization ◽

Alkane Hydroxylase ◽

Photosynthetic Membrane ◽

Intracytoplasmic Membrane ◽

Light Harvesting Complexes ◽

Pigment Protein Complexes

ABSTRACT The Rhodobacter sphaeroides intracytoplasmic membrane (ICM) is an inducible membrane that is dedicated to the major events of bacterial photosynthesis, including harvesting light energy, separating primary charges, and transporting electrons. In this study, multichromatographic methods coupled with Fourier transform ion cyclotron resonance mass spectrometry, combined with subcellular fractionation, was used to test the hypothesis that the photosynthetic membrane of R. sphaeroides 2.4.1 contains a significant number of heretofore unidentified proteins in addition to the integral membrane pigment-protein complexes, including light-harvesting complexes 1 and 2, the photochemical reaction center, and the cytochrome bc 1 complex described previously. Purified ICM vesicles are shown to be enriched in several abundant, newly identified membrane proteins, including a protein of unknown function (AffyChip designation RSP1760) and a possible alkane hydroxylase (RSP1467). When the genes encoding these proteins are mutated, specific photosynthetic phenotypes are noted, illustrating the potential new insights into solar energy utilization to be gained by this proteomic blueprint of the ICM. In addition, proteins necessary for other cellular functions, such as ATP synthesis, respiration, solute transport, protein translocation, and other physiological processes, were also identified to be in association with the ICM. This study is the first to provide a more global view of the protein composition of a photosynthetic membrane from any source. This protein blueprint also provides insights into potential mechanisms for the assembly of the pigment-protein complexes of the photosynthetic apparatus, the formation of the lipid bilayer that houses these integral membrane proteins, and the possible functional interactions of ICM proteins with activities that reside in domains outside this specialized bioenergetic membrane.

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