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Translocation Pathway (translocation + pathway)

Distribution by Scientific Domains

Life Sciences	100%

Selected Abstracts

Translocation of proteins across archaeal cytoplasmic membranes

FEMS MICROBIOLOGY REVIEWS, Issue 1 2004
Mechthild Pohlschröder
Abstract All cells need to transport proteins across hydrophobic membranes. Several mechanisms have evolved to facilitate this transport, including: (i) the universally-conserved Sec system, which transports proteins in an unfolded conformation and is thought to be the major translocation pathway in most organisms and (ii) the Tat system, which transports proteins that have already obtained some degree of tertiary structure. Here, we present the current understanding of these processes in the domain Archaea, and how they compare to the corresponding pathways in bacteria and eukaryotes. [source]

The structural view of bacterial translocation-specific chaperone SecB: implications for function

MOLECULAR MICROBIOLOGY, Issue 2 2005
Jiahai Zhou
Summary SecB is a molecular chaperone that functions in bacterial post-translational protein translocation pathway. It maintains newly synthesized precursor polypeptide chains in a translocation-competent state and guides them to the translocon via its high-affinity binding to the ligand as well as to the membrane-embedded ATPase SecA. Recent advances in elucidating the structures of SecB have enabled the examination of protein function in the structural context. Structures of SecB from both Haemophilus influenzae and Escherichia coli support the early two-subsite polypeptide-binding model. In addition, the detailed molecular interaction between SecB and SecA was revealed by a structure of SecB in complex with the C-terminal zinc-containing domain of SecA. These observations explain the dual role of SecB plays in the translocation pathway, as a molecular chaperone and a specific targeting factor. A model of SecB,SecA complex suggests that the binding of SecA to SecB changes the conformation of the polypeptide binding sites in the chaperone, enabling transfer of precursor polypeptides from SecB to SecA. Recent studies also show the presence of a second zinc-independent SecB binding site in SecA and the new interaction might contribute to the function of SecB. [source]

Pathogen-induced resistance and alarm signals in the phloem

MOLECULAR PLANT PATHOLOGY, Issue 5 2004
AART J. E. VAN BEL
SUMMARY Despite a long-standing notion of long-distance signals triggering systemic acquired resistance (SAR), the translocation pathway and the identity of the signals involved have not been determined with any degree of certainty. A critical assessment indicates that, in parallel to signalling via the phloem, alternative modes for SAR induction such as signalling via the xylem or air-borne signalling by volatile substances may occur. This review further evaluates several classes of compounds as being functional in systemic resistance signalling. Evidence in favour of SAR involvement of phloem-mobile substances such as salicylic acid, lipid-derived molecules, reactive oxygen species and components of the antioxidant machinery is contradictory, circumstantial or inconclusive, at best. Nitric oxide bound to proteins or thiols seems a good candidate for signalling, but has not been found in phloem sap thus far. No convincing support of the involvement in SAR of phloem-mobile substances such as calcium, oligosaccharides, peptides or RNA species, which function in other systemic signalling cascades, has yet been produced. Nevertheless, phloem-mobile macromolecules are considered as potential tools for SAR given their pivotal role in remote gene expression under stress conditions. In this framework, the existence of several cascades for signal generation along the phloem pathway is envisaged. Finally, recent methods for detection of molecular signals in phloem sap and their expression in companion cells are presented. [source]