TY - JOUR
KW - Amino Acid Sequence
KW - Arabidopsis
KW - Arabidopsis Proteins
KW - Bacteriophages
KW - DNA-Binding Proteins
KW - DNA-Directed RNA Polymerases
KW - Gene Expression Regulation, Plant
KW - Gene Library
KW - Intracellular Membranes
KW - Light
KW - Molecular Sequence Data
KW - Organ Specificity
KW - Promoter Regions, Genetic
KW - Protein Binding
KW - Protein Transport
KW - RNA, Messenger
KW - RNA, Ribosomal, 16S
KW - Saccharomyces cerevisiae Proteins
KW - Thylakoids
KW - Transcription Factors
KW - Two-Hybrid System Techniques
AU - Jacinthe Azevedo
AU - Florence Courtois
AU - Mohamed-Ali Hakimi
AU - Emilie Demarsy
AU - Thierry Lagrange
AU - Jean-Pierre Alcaraz
AU - Pankaj Jaiswal
AU - Laurence Maréchal-Drouard
AU - Silva Lerbs-Mache
AB - The plastid genome of dicotyledonous plants is transcribed by three different RNA polymerases; an eubacterial-type enzyme, PEP; and two phage-type enzymes, RPOTp and RPOTmp. RPOTp plays an important role in chloroplast transcription, biogenesis, and mesophyll cell proliferation. RPOTmp fulfills a specific function in the transcription of the rrn operon in proplasts/amyloplasts during seed imbibition/germination and a more general function in chloroplasts during later developmental stages. In chloroplasts, RPOTmp is tightly associated with thylakoid membranes indicating that functional switching of RPOTmp is connected to thylakoid association. By using the yeast two-hybrid system, we have identified two proteins that interact with RPOTmp. The two proteins are very similar, both characterized by three N-terminal transmembrane domains and a C-terminal RING domain. We show that at least one of these proteins is an intrinsic thylakoid membrane protein that fixes RPOTmp on the stromal side of the thylakoid membrane, probably via the RING domain. A model is presented in which light by triggering the synthesis of the RING protein determines membrane association and functional switching of RPOTmp.
BT - Proceedings of the National Academy of Sciences of the United States of America
C1 - http://www.ncbi.nlm.nih.gov/pubmed/18567673?dopt=Abstract
DA - 2008 Jul 1
IS - 26
J2 - Proc. Natl. Acad. Sci. U.S.A.
LA - eng
N2 - The plastid genome of dicotyledonous plants is transcribed by three different RNA polymerases; an eubacterial-type enzyme, PEP; and two phage-type enzymes, RPOTp and RPOTmp. RPOTp plays an important role in chloroplast transcription, biogenesis, and mesophyll cell proliferation. RPOTmp fulfills a specific function in the transcription of the rrn operon in proplasts/amyloplasts during seed imbibition/germination and a more general function in chloroplasts during later developmental stages. In chloroplasts, RPOTmp is tightly associated with thylakoid membranes indicating that functional switching of RPOTmp is connected to thylakoid association. By using the yeast two-hybrid system, we have identified two proteins that interact with RPOTmp. The two proteins are very similar, both characterized by three N-terminal transmembrane domains and a C-terminal RING domain. We show that at least one of these proteins is an intrinsic thylakoid membrane protein that fixes RPOTmp on the stromal side of the thylakoid membrane, probably via the RING domain. A model is presented in which light by triggering the synthesis of the RING protein determines membrane association and functional switching of RPOTmp.
PY - 2008
SP - 9123
EP - 8
T2 - Proceedings of the National Academy of Sciences of the United States of America
TI - Intraplastidial trafficking of a phage-type RNA polymerase is mediated by a thylakoid RING-H2 protein.
VL - 105
SN - 1091-6490
ER -