Characterisation of acyltransferases from Synechocystis sp. PCC6803

Weier, Dagmar; Müller, Cláudia; Gaspers, Claudia; Frentzen, Margrit

doi:10.1016/j.bbrc.2005.06.197

Cited by 38 publications

(36 citation statements)

References 31 publications

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“…Therefore, the phycobilisome complex in D1848 D2060 cells could be susceptible to protein extraction under our conditions. As previously reported by Weier et al (2005), we herein confirmed that sll1848 encodes the major LPAAT of Synechocystis sp. PCC6803 required for maintaining C16 fatty acids in the sn-2 positions of membrane lipids.…”

Section: Pcc6803 Cellssupporting

confidence: 91%

“…Although cyanobacterial acyltransferases are likely to use acyl-acyl carrier protein (acyl-ACP) in vivo (Lem and Stumpf, 1984;Weier et al, 2005), acyl-CoA substrates were sufficient to detect LPAAT activities. In most cases, acyltransferase shows similar fatty acid specificity for acyl-CoA substrates as for acyl-ACP (Bertrams and Heinz, 1981;Frentzen et al, 1983).…”

Section: Pcc6803 Cellsmentioning

confidence: 99%

“…We conclude that C16 fatty acids in the sn-2 positions of glycerolipids have some advantages for the photosynthetic growth of this cyanobacterium. The third acyltransferase slr2060, which was recently found to be a lysophospholipid acyltransferase (Weier et al, 2005), exhibited neither GPAT nor LPAAT activities. We discuss the evolutionary significance of the different types of acyltransferases in cyanobacteria and higher photosynthetic eukaryotes.…”

mentioning

confidence: 93%

“…According to this criterion, GPAT and LPAAT genes have been identified in Arabidopsis (Arabidopsis thaliana; Zheng et al, 2003;Kim and Huwang, 2004;Yu et al, 2004) and Synechocystis sp. PCC6803 (Weier et al, 2005).…”

mentioning

confidence: 99%

“…PCC6803 contains three candidate genes for acyltransferases: sll1848, sll1752, and slr2060. Weier et al (2005) reported recently that sll1848 encodes the major, indispensable LPAAT specific to palmitate (16:0). However, here we show that sll1848 is dispensable and that its disruptants, D1848 or D1848 D2060 cells, exhibit dramatically higher contents of stearate (18:0), oleate (18:1), and linoleate (18:2) in place of 16:0 in the sn-2 positions of glycerolipids.…”

mentioning

confidence: 99%

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The Significance of C16 Fatty Acids in the sn-2 Positions of Glycerolipids in the Photosynthetic Growth of Synechocystis sp. PCC6803

et al. 2006

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Most extant cyanobacteria contain C16 fatty acids in the sn-2 positions of glycerolipids, which are regulated by lysophosphatidic acid acyltransferase (LPAAT; EC 2.3.1.51). Synechocystis sp. PCC6803 contains sll1848, sll1752, and slr2060 as putative acyltransferase genes. sll1848 was recently reported to encode an indispensable palmitoyl-specific LPAAT; however, here we show that each of the three genes is dispensable. D1848 and D1848 D2060 cells had markedly higher contents of stearate (18:0), oleate (18:1), and linoleate (18:2) in place of palmitate (16:0) in the sn-2 positions, suggesting that D1848 D2060 cells incorporate 18:0 and 18:1 in the sn-2 positions. The levels of sll1752 transcripts increased in D1848 D2060 cells. This was accompanied by increased LPAAT activity toward 18:0 coenzyme A and its derivative in the membrane fraction. From these findings, together with the activity of a recombinant sll1752 protein and complementation of the Escherichia coli LPAAT mutant plsC, we conclude that sll1752 encodes a second LPAAT that prefers stearoyl and oleoyl substrates. D1848 D2060 cells grew slowly at 30°C at lower cell density, and exhibited more severe damage at 20°C than wild-type cells. Furthermore, D1848 D2060 cells exhibited photoinhibition more severely than wild-type cells. A phycobilisome core-membrane linker protein (slr0335) was also found to be susceptible to protein extraction under our conditions; its content decreased in the membrane fractions of D1848 D2060 cells. We conclude that C16 fatty acids in sn-2 positions are preferred in the photosynthetic growth of this cyanobacterium, despite sll1752 orthologs being conserved in most cyanobacteria. However, no sll1752 ortholog is conserved among photosynthetic eukaryotes including Cyanidioschyzon merolae.

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Section: Pcc6803 Cellssupporting

confidence: 91%