Update in nucleotide-dependent processes in plant chloroplasts
2008 (English)In: Current Knowledge in Plant Cell Compartments / [ed] Spetea, C.Thuswaldner, S., Kerala: Research Signpost Publisher , 2008, 105-149 p.Chapter in book (Other academic)
Chloroplasts are photosynthetically active plastids found in all green plant cells. They have two types of membranes, the double envelope membrane surrounding the organelle and the thylakoid membrane containing the photosynthetic machinery. The envelope membrane represents the interface between the cytosol and chloroplast stroma, whereas the thylakoid membrane is the interface between the stroma and the lumenal space. This chapter attempts to give an update in nucleotide-dependent processes in plant chloroplasts. The current knowledge is that ATP is produced in the light-dependent photosynthetic reactions in the thylakoid membrane, and is used during CO2-fixation in the stroma as well as in the energy-dependent processes occurring on the thylakoid and envelope membranes. There is also increasing evidence that the thylakoid lumen is a chloroplast compartment with an unexpectedly active nucleotide metabolism, expanding its function beyond a bioenergetic perspective. Here we will discuss three distinct classes of chloroplast nucleotide-binding proteins: (i) transporters involved in ATP synthesis, translocation and utilization; (ii) nucleoside diphosphate kinases, involved in conversion of ATP to other nucleotides; and (iii) GTP-binding proteins, using the energy of GTP hydrolysis to drive various processes during chloroplast biogenesis, function and turnover. The main aspects reviewed for each chloroplast protein will be prediction, proteomic and/or individual identification, in vitro biochemical characterization and in planta functional analysis.
Place, publisher, year, edition, pages
Kerala: Research Signpost Publisher , 2008. 105-149 p.
National CategoryMedical and Health Sciences
IdentifiersURN: urn:nbn:se:liu:diva-14184ISBN: 978-81-308-0104-9OAI: oai:DiVA.org:liu-14184DiVA: diva2:22836