A GENETICALLY-ENGINEERED INCREASE IN FATTY-ACID UNSATURATION IN SYNECHOCOCCUS SP. PCC-7942 ALLOWS EXCHANGE OF D1 PROTEIN FORMS AND SUSTENANCE OF PHOTOSYSTEM-II ACTIVITY AT LOW-TEMPERATURE

Citation
K. Sippola et al., A GENETICALLY-ENGINEERED INCREASE IN FATTY-ACID UNSATURATION IN SYNECHOCOCCUS SP. PCC-7942 ALLOWS EXCHANGE OF D1 PROTEIN FORMS AND SUSTENANCE OF PHOTOSYSTEM-II ACTIVITY AT LOW-TEMPERATURE, European journal of biochemistry, 251(3), 1998, pp. 641-648
Citations number
45
Categorie Soggetti
Biology
ISSN journal
00142956
Volume
251
Issue
3
Year of publication
1998
Pages
641 - 648
Database
ISI
SICI code
0014-2956(1998)251:3<641:AGIIFU>2.0.ZU;2-J
Abstract
Photosystem II (PSII)-reaction-center protein D1 is encoded by three p sbA genes in Synechococcus sp. PCC 7942. The psbA gene encodes D1 form I (D1:1) and the psbAIII and pshAlll genes encode the transiently exp ressed D1 form II (D1:2). We have studied the role of membrane-lipid u nsaturation in the expression of psbA genes at low temperature, using a Synechococcus transformant with an increased unsaturation level of m embrane lipids.Transfer of the cells from 32 degrees C to 25 degrees C under growth light resulted in the exchange of D1:1, the prevailing f orm, for D1:2 in the wild- type bacterium and the transformant, with n o loss of PSII activity.Lowering the temperature further to 18 degrees C caused a drastic decrease in PSII activity in the wild-type bacteri um, whereas the transformant was much less affected. Similar decreases in psbAI transcripts and loss of D1 : 1 occurred in both strains at 1 8 degrees C, with concomitant accumulation of psbAII/III transcripts, the latter event being especially prominent in the wild-type bacterium . However, the wild-type bacterium was incapable of accumulating D1:2 to compensate for the loss of D1:l, which resulted in disassembly of P SII at low temperature. These results imply translational rather than transcriptional regulation of psbA gene expression in Synechococcus 79 42 at low temperature, and demonstrate the crucial role of the degree of membrane-lipid unsaturation in promotion of exchange of the D1 prot ein forms and thus the sustenance of PSII function at low temperature.