Identification of secreted proteins of the cyanobacterium Synechocystis sp. strain PCC 6803

Sergeyenko, Tatiana V

doi:10.1016/s0378-1097(00)00482-1

Cited by 10 publications

(17 citation statements)

References 10 publications

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“…In the previous study we identified PilA1 as the major secreted protein of Synechocystis [15]. The deduced amino acid sequence of the leader peptide of PilA1 (Sll1694) was used in this study to elucidate its actual ability to secrete proteins into culture medium.…”

Section: Discussionmentioning

confidence: 99%

“…The supernatant was re‐centrifuged and filtered through a Stericap filter unit. Isolation of secreted proteins from the culture medium was performed as described earlier[15]. Proteins were separated by electrophoresis in 12% SDS–PAGE and in parallel, in 12% SDS–PAGE that contained 0.2% of lichenan.…”

Section: Methodsmentioning

confidence: 99%

“…Recently, we identified seven proteins of Synechocystis sp. PCC 6803 that are secreted into the culture medium under normal growth conditions[15]. The major secreted protein identified appeared to be PilA1 – the structural component of pili.…”

Section: Introductionmentioning

confidence: 99%

“…We have found several homologs of PilA1 in the genome of Synechocystis . They are characterized by a high degree of homology only in short hydrophobic regions that represent the N‐terminal parts of mature pilin‐like proteins[15]. No significant homology has been observed in the putative leader peptides of those proteins.…”

Section: Introductionmentioning

confidence: 99%

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Cyanobacterial leader peptides for protein secretion

Sergeyenko¹,

Los²

2003

FEMS Microbiology Letters

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The leader peptide of the major secreted protein PilA1 of the cyanobacterium Synechocystis sp. strain PCC 6803 and several artificial leader peptides have been used to study secretion of the reporter protein lichenase to the culture medium. The strains of Synechocystis carrying lichenase with the leader sequences of PilA and with the leader sequence of Slr2016 efficiently secreted the reporter protein. The artificial leader sequence that was characterized by the overall positive charge (as PilA1 and Slr2016 leaders) also allowed secretion. The artificial leader with negative charge, however, did not allow secretion of the reporter protein. Moreover, no secreted proteins have been isolated from this strain using conventional techniques for preparation of secreted proteins. These data suggest that the general secretion pathway in cyanobacteria, at least for pilins, recognizes the overall charge of the leader sequences, and operates in a sequence-non-specific manner. ß

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cyanobacterial leader peptides for protein secretion

Sergeyenko¹,

Los²

2003

FEMS Microbiology Letters

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“…Several cyanobacteria produce extracellular metabolites, such as polypeptides (Sergeyenko and Los 2000) and polysaccharides (De Philippis and Vincenzini 1998;Otero and Vincenzini 2003). Our results show that, Oscillatoria sp.…”

Section: Discussionmentioning

confidence: 62%

Extracellular phycoerythrin-like protein released by freshwater cyanobacteria Oscillatoria and Scytonema sp.

et al. 2009

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During growth of the freshwater cyanobacteria, Oscillatoria sp. BTCC/A0004, and Scytonema sp. TISTR 8208, a pink pigment is released into the growth medium. The pigment from each source had a molecular weight of approximately 250 kDa and had adsorption maxima at 560 and 620 nm. These results suggest that pink pigment is a phycoerythrin-like protein. It inhibited the growth of green algae, Chlorella fusca and Chlamydomonas reinhardtii, but not other cyanobacteria or true bacteria. The concentration at which growth inhibition 50% occurred was 0.5, 6 and more than 10 mg ml(-1), respectively.

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Proximity-based proteomics reveals the thylakoid lumen proteome in the cyanobacterium Synechococcus sp. PCC 7002

et al. 2020

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Cyanobacteria possess unique intracellular organization. Many proteomic studies have examined different features of cyanobacteria to learn about the intracellular structures and their respective functions. While these studies have made great progress in understanding cyanobacterial physiology, the conventional fractionation methods used to purify cellular structures have limitations; specifically, certain regions of cells cannot be purified with existing fractionation methods. Proximity-based proteomics techniques were developed to overcome the limitations of biochemical fractionation for proteomics. Proximity-based proteomics relies on spatiotemporal protein labeling followed by mass spectrometry of the labeled proteins to determine the proteome of the region of interest. We performed proximity-based proteomics in the cyanobacterium Synechococcus sp. PCC 7002 with the APEX2 enzyme, an engineered ascorbate peroxidase. We determined the proteome of the thylakoid lumen, a region of the cell that has remained challenging to study with existing methods, using a translational fusion between APEX2 and PsbU, a lumenal subunit of photosystem II. Our results demonstrate the power of APEX2 as a tool to study the cell biology of intracellular features and processes, including photosystem II assembly in cyanobacteria, with enhanced spatiotemporal resolution.

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Identification of secreted proteins of the cyanobacterium Synechocystis sp. strain PCC 6803

Cited by 10 publications

References 10 publications

Cyanobacterial leader peptides for protein secretion

Cyanobacterial leader peptides for protein secretion

Extracellular phycoerythrin-like protein released by freshwater cyanobacteria Oscillatoria and Scytonema sp.

Proximity-based proteomics reveals the thylakoid lumen proteome in the cyanobacterium Synechococcus sp. PCC 7002

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