A cyanobacterium which lacks thylakoids

Rippka, Rosmarie; Waterbury, John; Cohen-Bazire, Germaine

doi:10.1007/bf00446333

Cited by 303 publications

(205 citation statements)

References 15 publications

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“…Because G. violaceus PCC7421 has no orthologs for sll1752, other LPAATs must be responsible for the unique fatty acid composition of this cyanobacterium. Interestingly, G. violaceus PCC7421 exhibits relatively slow growth under photosynthetic conditions and is sensitive to strong light (Rippka et al, 1974). These features are similar to those found in D1848 D2060 cells, although G. violaceus PCC7421 also lacks SQDG.…”

Section: Evolution Of Cyanobacterial Lpaatsupporting

confidence: 57%

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: Evolution Of Cyanobacterial Lpaatsupporting

confidence: 57%

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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“…Based on the examination of isolated phycobilisomes by electron microscopy, different morphological types were described: hemi-ellipsoidal, hemi-discoidal, block shaped and bundle shaped (for a review, see Sidler 1994). The latter type, which forms a cortical layer on the inner surface of the cytoplasmic membrane, was only found in an unusual cyanobacterium Gloeobacter violaceus that does not possess thylakoids (Rippka et al 1974;Guglielmi et al 1981). Gantt and Lipschultz (1974) initially reported that phycobilisomes isolated from Porphyridium cruentum only consisted of phycobiliproteins with 84% B-and b-phycoerythrin, 11% R-phycocyanin and 5% allophycocyanin.…”

Section: The Phycobilisome: a Supramolecular Complexmentioning

confidence: 99%

Phycobiliproteins and phycobilisomes: the early observations

Marsac

2005

Discoveries in Photosynthesis

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The purpose of this minireview is to highlight the early observations that led to the discovery of the physicochemical properties of the phycobiliproteins, their structure and function, and to their architectural organization in supramolecular complexes, the phycobilisomes. Generally attached on the stromal surface of the thylakoid membranes in both prokaryotic (cyanobacteria) and eukaryotic cells (cyanelles, red algae and cryptomonads), these complexes represent the most abundant soluble proteins and the major light-harvesting antennae for photosynthesis. This review mainly focuses on the years prior to the development of the molecular biology of cyanobacteria that flourished in the 1980s. We refer the reader to the comprehensive and excellent review by Sidler (1994) for more recent discoveries and more detailed literature on this topic.

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“…A specific staining method, employing the Sakaguchi reaction (Fogg, 1951 ;Baker, 1947), was used to identify cyanophycin granules. The techniques for the preparation of specimens and their examination by electron microscopy are described elsewhere (Rippka, Waterbury & Cohen-Bazire, 1974).…”

Section: Anaerobic Nitrogenase Synthesis By Cyanobacteria 85mentioning

confidence: 99%