Search results for "PspA"
showing 6 items of 6 documents
Functional Implications of Multiple IM30 Oligomeric States
2019
The inner membrane-associated protein of 30 kDa (IM30), also known as the vesicle-inducing protein in plastids 1 (Vipp1), is essential for photo-autotrophic growth of cyanobacteria, algae and higher plants. While its exact function still remains largely elusive, it is commonly accepted that IM30 is crucially involved in thylakoid membrane biogenesis, stabilization and/or maintenance. A characteristic feature of IM30 is its intrinsic propensity to form large homo-oligomeric protein complexes. 15 years ago, it has been reported that these supercomplexes have a ring-shaped structure. However, the in vivo significance of these ring structures is not finally resolved yet and the formation of mor…
Membrane chaperoning by members of the PspA/IM30 protein family
2017
ABSTRACTPspA, IM30 (Vipp1) and LiaH, which all belong to the PspA/IM30 protein family, form high molecular weight oligomeric structures. For all proteins membrane binding and protection of the membrane structure and integrity has been shown or postulated. Here we discuss the possible membrane chaperoning activity of PspA, IM30 and LiaH and propose that larger oligomeric structures bind to stressed membrane regions, followed by oligomer disassembly and membrane stabilization by protein monomers or smaller/different oligomeric scaffolds.
Mg2+ binding triggers rearrangement of the IM30 ring structure, resulting in augmented exposure of hydrophobic surfaces competent for membrane binding
2018
The "inner membrane-associated protein of 30 kDa" (IM30), also known as "vesicle-inducing protein in plastids 1" (Vipp1), is found in the majority of photosynthetic organisms that use oxygen as an energy source, and its occurrence appears to be coupled to the existence of thylakoid membranes in cyanobacteria and chloroplasts. IM30 is most likely involved in thylakoid membrane biogenesis and/or maintenance, and has recently been shown to function as a membrane fusion protein in presence of Mg2+ However, the precise role of Mg2+ in this process and its impact on the structure and function of IM30 remains unknown. Here, we show that Mg2+ binds directly to IM30 with a binding affinity of ∼1 mm …
Quantum Real - Time Turing Machine
2001
The principles of quantum computation differ from the principles of classical computation very much. Quantum analogues to the basic constructions of the classical computation theory, such as Turing machine or finite 1-way and 2-ways automata, do not generalize deterministic ones. Their capabilities are incomparable. The aim of this paper is to introduce a quantum counterpart for real - time Turing machine. The recognition of a special kind of language, that can't be recognized by a deterministic real - time Turing machine, is shown.
Space-Efficient 1.5-Way Quantum Turing Machine
2001
1.5QTM is a sort of QTM (Quantum Turing Machine) where the head cannot move left (it can stay where it is and move right). For computations is used other - work tape. In this paper will be studied possibilities to economize work tape space more than the same deterministic Turing Machine can do (for some of the languages). As an example language (0i1i|i ≥ 0) is chosen, and is proved that this language could be recognized by deterministic Turing machine using log(i) cells on work tape , and 1.5QTM can recognize it using constant cells quantity.
Organization into higher-ordered ring structures counteracts membrane binding of IM30, a protein associated with inner membranes in chloroplasts and …
2017
ABSTRACT PspA, IM30 (Vipp1) and LiaH, which all belong to the PspA/IM30 protein family, form high molecular weight oligomeric structures. For all proteins membrane binding and protection of the membrane structure and integrity has been shown or postulated. Here we discuss the possible membrane chaperoning activity of PspA, IM30 and LiaH and propose that larger oligomeric structures bind to stressed membrane regions, followed by oligomer disassembly and membrane stabilization by protein monomers or smaller/different oligomeric scaffolds.