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B Bölter

Publications and source records attributed to B Bölter.

5 recordsLinked to original sources
PubMed1999

A rectifying ATP-regulated solute channel in the chloroplastic outer envelope from pea.

Phosphorylated carbohydrates are the main photoassimilated export products from chloroplasts that support the energy household and metabolism of the plant cell. Channels formed by the chloroplastic outer envelope protein OEP21 selectively facilitate the translocation of triosephosphate, 3-phosphoglycerate and phosphate, central intermediates in the source-sink relationship between the chloroplast and the cytosol. The anion selectivity and asymmetric transport properties of OEP21 are modulated by the ratio between ATP and triosephosphates, 3-phosphoglycerate and phosphate in the intermembrane space. Conditions that lead to export of triosephosphate from chloroplasts, i.e. photosynthesis, result in outward-rectifying OEP21 channels, while a high ATP to triosephosphate ratio, e.g. dark metabolism, leads to inward-rectifying OEP21 channels with a less pronounced anion selectivity. We conclude that solute exchange between plastids and cytosol can already be regulated at the level of the organellar outer membrane.

Adenosine Triphosphate↗
PubMed1998

Origin of a chloroplast protein importer.

During evolution, chloroplasts have relinquished the majority of their genes to the nucleus. The products of transferred genes are imported into the organelle with the help of an import machinery that is distributed across the inner and outer plastid membranes. The evolutionary origin of this machinery is puzzling because, in the putative predecessors, the cyanobacteria, the outer two membranes, the plasma membrane, and the lipopolysaccharide layer lack a functionally similar protein import system. A 75-kDa protein-conducting channel in the outer envelope of pea chloroplasts, Toc75, shares approximately 22% amino acid identity to a similarly sized protein, designated SynToc75, encoded in the Synechocystis PCC6803 genome. Here we show that SynToc75 is located in the outer membrane (lipopolysaccharide layer) of Synechocystis PCC6803 and that SynToc75 forms a voltage-gated, high conductance channel with a high affinity for polyamines and peptides in reconstituted liposomes. These findings suggest that a component of the chloroplast protein import system, Toc75, was recruited from a preexisting channel-forming protein of the cyanobacterial outer membrane. Furthermore, the presence of a protein in the chloroplastic outer envelope homologous to a cyanobacterial protein provides support for the prokaryotic nature of this chloroplastic membrane.

Amino Acid Sequence↗
PubMed1998

A protein import receptor in pea chloroplasts, Toc86, is only a proteolytic fragment of a larger polypeptide.

The protein import complex of the chloroplastic outer envelope (Toc-complex) contains a prominent subunit of 86 kDa molecular weight (Toc86). Toc86 was identified as a putative precursor receptor. The Arabidopsis genome sequencing project indicates that Toc86 represents only a proteolytic fragment of a larger polypeptide of 160 kDa. The 160-kDa protein, which we name Toc160, is only present in significant amounts in pea chloroplasts isolated under stringent conditions. The capacity of chloroplasts to import an in vitro translated precursor protein correlates well with the integrity of Toc160. We conclude that Toc160 is still a bonafide subunit of the protein import machinery of chloroplasts.

Amino Acid Sequence↗