Molecular basis for membrane phospholipid diversity: why are there so many lipids?

W Dowhan - Annual review of biochemistry, 1997 - annualreviews.org
Phospholipids play multiple roles in cells by establishing the permeability barrier for cells
and cell organelles, by providing the matrix for the assembly and function of a wide variety of …

The complete general secretory pathway in gram-negative bacteria

AP Pugsley - Microbiological reviews, 1993 - Am Soc Microbiol
The unifying feature of all proteins that are transported out of the cytoplasm of gram-negative
bacteria by the general secretory pathway (GSP) is the presence of a long stretch of …

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion

A Economou, W Wickner - Cell, 1994 - cell.com
SecA, the peripheral subunit of E. coli preprotein translocase, alternates between a
membrane inserted and a deinserted state as part of the catalytic cycle of preprotein …

Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes

TA Rapoport, B Jungnickel… - Annual review of …, 1996 - annualreviews.org
Protein transport across the endoplasmic reticulum membrane can occur by two pathways, a
co-and a post-translational one. In both cases, polypeptides are first targeted to translocation …

Functions of the gene products of Escherichia coli

M Riley - Microbiological reviews, 1993 - Am Soc Microbiol
A list of currently identified gene products of Escherichia coli is given, together with a
bibliography that provides pointers to the literature on each gene product. A scheme to …

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF

A Economou, JA Pogliano, J Beckwith, DB Oliver… - Cell, 1995 - cell.com
The SecA subunit of E. coli preprotein translocase promotes protein secretion during cycles
of membrane insertion and deinsertion at SecYEG. This process is regulated both by …

Two distinct ATP‐binding domains are needed to promote protein export by Escherichia coli SecA ATPase

C Mitchell, D Oliver - Molecular microbiology, 1993 - Wiley Online Library
Six putative ATP‐binding motifs of SecA protein were altered by oligonucleotide‐directed
mutagenesis to try to define the ATP‐binding regions of this multifunctional protein. The …

SecD is involved in the release of translocated secretory proteins from the cytoplasmic membrane of Escherichia coli.

S Matsuyama, Y Fujita, S Mizushima - The EMBO Journal, 1993 - embopress.org
The SecD protein is one of the components that has been suggested from genetic studies to
be involved in the protein secretion across the cytoplasmic membrane of Escherichia coli …

[HTML][HTML] Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane

E Or, A Navon, T Rapoport - The EMBO journal, 2002 - embopress.org
The ATPase SecA mediates post-translational translocation of precursor proteins through
the SecYEG channel of the bacterial inner membrane. We show that SecA, up to now …

The C Terminus of SecA Is Involved in Both Lipid Binding and SecB Binding (∗)

E Breukink, N Nouwen, A van Raalte… - Journal of Biological …, 1995 - ASBMB
Using C-terminal deletion mutations in secA, we localized the previously proposed
(Breukink, E., Keller, RCA, and de Kruijff, B.(1993), FEBS Lett. 331, 19-24) second lipid …