TY - JOUR
T1 - Transcriptional profiles and structural models of the Synechocystis sp. PCC 6803 Deg proteases
AU - Jansén, Tove
AU - Kidron, Heidi
AU - Taipaleenmäki, Hanna
AU - Salminen, Tiina
AU - Mäenpää, Pirkko
PY - 2005/6
Y1 - 2005/6
N2 - The Synechocystis sp. PCC 6803 genome harbours a deg gene family consisting of three members, degP (htrA, slr1204), degQ (hhoA, sll1679) and degS (hhoB, sll1427). We studied the environmental regulation of the Synechocystis sp. PCC 6803 deg genes at the level of transcription and protein structures of the gene products to evaluate their hypothetical role in D1 protein turnover. Northern blotting showed that transcription of the deg genes is differentially regulated, supporting a view of distinct roles of Degs in cellular processes. The oligomerization state as well as the three dimensional structures of the Synechocystis sp. PCC 6803 Deg proteases were predicted based on an amino acid sequence alignment and comparison of the Deg crystal structures from human, Escherichia coli and Thermotoga maritima. The structures of the Synechocystis sp. PCC 6803 Degs resemble more the Thermotoga maritima Deg enzyme structure than the Escherichia coli one. Moreover, the structures of the LA-loops hint towards a homotrimeric form of the Synechocystis sp. PCC 6803 Deg proteases.
AB - The Synechocystis sp. PCC 6803 genome harbours a deg gene family consisting of three members, degP (htrA, slr1204), degQ (hhoA, sll1679) and degS (hhoB, sll1427). We studied the environmental regulation of the Synechocystis sp. PCC 6803 deg genes at the level of transcription and protein structures of the gene products to evaluate their hypothetical role in D1 protein turnover. Northern blotting showed that transcription of the deg genes is differentially regulated, supporting a view of distinct roles of Degs in cellular processes. The oligomerization state as well as the three dimensional structures of the Synechocystis sp. PCC 6803 Deg proteases were predicted based on an amino acid sequence alignment and comparison of the Deg crystal structures from human, Escherichia coli and Thermotoga maritima. The structures of the Synechocystis sp. PCC 6803 Degs resemble more the Thermotoga maritima Deg enzyme structure than the Escherichia coli one. Moreover, the structures of the LA-loops hint towards a homotrimeric form of the Synechocystis sp. PCC 6803 Deg proteases.
KW - Amino Acid Sequence
KW - Gene Expression Profiling
KW - Gene Expression Regulation, Bacterial
KW - Models, Molecular
KW - Molecular Sequence Data
KW - Multigene Family
KW - Peptide Hydrolases/chemistry
KW - Protein Conformation
KW - Sequence Homology, Amino Acid
KW - Synechocystis/enzymology
KW - Transcription, Genetic
U2 - 10.1007/s11120-005-0475-x
DO - 10.1007/s11120-005-0475-x
M3 - Article
C2 - 16049755
SN - 0166-8595
VL - 84
SP - 57
EP - 63
JO - Photosynthesis Research
JF - Photosynthesis Research
IS - 1-3
ER -