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

Article Abstract:

Insertion and deinsertion of the SecA subunit of the Escherichia coli preprotein translocase at SecYEG is controlled by ATP binding and the SecD and SecF proteins. The deinserted SecA, which is bound to SecYEG, inserts into the SecYEG membrane after preprotein binding to SecA. The energy for the insertion is supplied by the ATP binding to the nucleotide-binding domain 1 (NBD1). Hydrolysis of ATP causes the deinsertion of SecA. The SecA membrane cycling is also controlled by translocase interaction between SecD and SecF. The binding of preprotein to SecA induces protein secretion.

Membrane fusion, Adenosine triphosphate, ATP, Cooperative binding (Biochemistry)

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LMA1 binds to vacuoles at Sec 18p (NSF), transfers upon ATP hydrolysis to a t-SNARE (Vam3p) complex, and is released during fusion

Article Abstract:

The role of the novel trafficking factor, low Mr activity 1 (LMA1), in vacoule fusion was investigated through assays with purified vacuoles from the Saccharomyces cerevisiae. LMA1 binding and release were characterized to further elucidate its role in vacuole fusion. Assays indicate that LMA1 binding to the vacuole requires the N-ethylmaleimide sensitive fusion (NSF) protein Sec18p, the soluble NSF attachment protein Sec17p and the guanosine triphosphate binding protein Ypt7p. Results also suggest a possible role for the LMA1 in other intracellular events.

Carrier proteins, Transport proteins, Saccharomyces, Lysosomes, Cell interaction, Cell interactions

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Biogenesis of the gram-negative bacterial envelope

Article Abstract:

The 3-layered structure of the cell envelope of gram-negative bacteria, comprises a bilayer-based plasma membrane, peptidoglycan mesh, a periplasm of soluble proteins and an outer membrane with proteins and lipids. Discussion on how newly made cell surface components are sorted to the right compartments, is presented, concentrating on translocation across the inner membrane.

Gram-negative bacteria

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