The twin-arginine translocation system: A novel means of transporting folded proteins in chloroplasts and bacteria
UNSPECIFIED (2000) The twin-arginine translocation system: A novel means of transporting folded proteins in chloroplasts and bacteria. BIOLOGICAL CHEMISTRY, 381 (2). pp. 89-93. ISSN 1431-6730Full text not available from this repository.
Protein translocases have been characterised in several membrane systems and the translocation mechanisms have been shown to differ in critical respects. Nevertheless, the majority were believed to transport proteins only in a largely unfolded state, and this widespread characteristic was viewed as a likely evolutionary effort to minimise the diameter of translocation pore required, Within the last few years, however, studies on the chloroplast thylakoid membrane have revealed a novel class of protein translocase which possesses the apparently unique ability to transport fully-folded proteins across a tightly sealed energy-transducing membrane. A related system, (the twin-arginine translocation, or Tat system) has now been characterised in the Escherichia coli plasma membrane and considerations of its substrate specificity again point to its involvement in the transport of folded proteins. The emerging data suggest a critical involvement in many membranes for the biogenesis of two types of globular protein: those that are obliged to fold prior to translocation, and those that fold too tightly or rapidly for other types of protein translocase to handle.
|Item Type:||Journal Item|
|Subjects:||Q Science > QD Chemistry|
|Journal or Publication Title:||BIOLOGICAL CHEMISTRY|
|Publisher:||WALTER DE GRUYTER & CO|
|Official Date:||February 2000|
|Number of Pages:||5|
|Page Range:||pp. 89-93|
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