Fraternal twins

Article Abstract:

The transmembrane Sec channel or Sec translocon, a commonly used protein-transport route into and across the endoplastic reticulum of higher organisms and the cell membrane of bacteria functions by forming two identical dimer units with a distinct role. The analysis shows that a single SecY complex is sufficient to bind to SecA, though an active channel can be formed only by employing two SecY complexes, converting all the chemical energy into mechanical energy.

Analysis, Physiological aspects, Endoplasmic reticulum, Cell membranes, Gel permeation chromatography

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Oxygen at life's boundaries

Article Abstract:

The unfamiliar prism of atomic rather than amino-acid composition was applied to show the mystery behind the evolution of transmembrane proteins and communication between intracellular compartments or between cell and their environments. It is observed that as evolution from unicellular to multicellular organisms requires efficient communication between cells, the evolutionary step was similarly hindered by insufficient levels of [O.sub.2].

United Kingdom, Amino acid metabolism

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Going against the flow

Article Abstract:

The similarities between disparate membrane proteins, like active transporters and passive channels can be understood, due to the advent of structures for several ion-selective channels. Releasing co-transporters from the grip of enzyme theory could lead to a possible reunion of co-transporters and channels.

United States

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