Regulation of Manganese Uptake in <i>Synechocystis</i> 6803 by RfrA, a Member of a Novel Family of Proteins Containing a Repeated Five-Residues Domain

Chandler, Leeann E; Bartsevich, Victor V.; Pakrasi, Himadri B.

doi:10.1021/bi027113a

Cited by 30 publications

(28 citation statements)

References 35 publications

(47 reference statements)

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“…Analysis of the FraF amino acid sequence shows that it is a pentapeptide repeat protein, one of a family of proteins containing a repeated five-residue domain (50). FraF is homologous to other pentapeptide repeat proteins, such as HglK (51), HetL (52), and PatL (53), that are involved in heterocyst differentiation.…”

Section: Discussionmentioning

confidence: 99%

“…A prediction of the structure of FraF performed with the Phyre server (55) renders a structure very similar to that of HetL. In other bacteria, pentapeptide repeat proteins can be found in different cellular compartments, and reported functions range from inhibition of DNA gyrase (56) to regulation of manganese uptake (50). We cannot currently envisage a mechanism of action for FraF, but its genomic location might imply a relation to the positive filamentation proteins encoded in the fraC operon.…”

Section: Discussionmentioning

confidence: 99%

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Cluster of Genes That Encode Positive and Negative Elements Influencing Filament Length in a Heterocyst-Forming Cyanobacterium

Merino-Puerto

Herrero

Flores

2013

Journal of Bacteriology

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The filamentous, heterocyst-forming cyanobacteria perform oxygenic photosynthesis in vegetative cells and nitrogen fixation in heterocysts, and their filaments can be hundreds of cells long. In the model heterocyst-forming cyanobacterium Anabaena sp. strain PCC 7120, the genes in the fraC-fraD-fraE operon are required for filament integrity mainly under conditions of nitrogen deprivation. The fraC operon transcript partially overlaps gene all2395, which lies in the opposite DNA strand and ends 1 bp beyond fraE. Gene all2395 produces transcripts of 1.35 kb (major transcript) and 2.2 kb (minor transcript) that overlap fraE and whose expression is dependent on the N-control transcription factor NtcA. Insertion of a gene cassette containing transcriptional terminators between fraE and all2395 prevented production of the antisense RNAs and resulted in an increased length of the cyanobacterial filaments. Deletion of all2395 resulted in a larger increase of filament length and in impaired growth, mainly under N 2 -fixing conditions and specifically on solid medium. We denote all2395 the fraF gene, which encodes a protein restricting filament length. A FraF-green fluorescent protein (GFP) fusion protein accumulated significantly in heterocysts. Similar to some heterocyst differentiation-related proteins such as HglK, HetL, and PatL, FraF is a pentapeptide repeat protein. We conclude that the fraC-fraD-fraE¢fraF gene cluster (where the arrow indicates a change in orientation), in which cis antisense RNAs are produced, regulates morphology by encoding proteins that influence positively (FraC, FraD, FraE) or negatively (FraF) the length of the filament mainly under conditions of nitrogen deprivation. This gene cluster is often conserved in heterocystforming cyanobacteria.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Cluster of Genes That Encode Positive and Negative Elements Influencing Filament Length in a Heterocyst-Forming Cyanobacterium

Merino-Puerto

Herrero

Flores

2013

Journal of Bacteriology

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“…The HT3ΔQ strain was previously reported (9). The HT3ΔO strain was generated by transforming the HT3 strain by using the ΔO construct previously reported (49). Purification of tagged PSII complexes was performed as described previously (3) with minor modifications.…”

Section: Methodsmentioning

confidence: 99%

MS-based cross-linking analysis reveals the location of the PsbQ protein in cyanobacterial photosystem II

Liu¹,

Zhang

Weisz

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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PsbQ is a luminal extrinsic protein component that regulates the water splitting activity of photosystem II (PSII) in plants, algae, and cyanobacteria. However, PsbQ is not observed in the currently available crystal structures of PSII from thermophilic cyanobacteria. The structural location of PsbQ within the PSII complex has therefore remained unknown. Here, we report chemical cross- D of CP47. We further show that genetic deletion of the psbO gene results in the complete absence of PsbQ in PSII complexes as well as the loss of the dimeric form of PSII. Overall, our data provide a molecular-level description of the enigmatic binding site of PsbQ in PSII in a cyanobacterium. These results also help us understand the sequential incorporation of the PsbQ protein during the PSII assembly process, as well as its stabilizing effect on the oxygen evolution activity of PSII.photosystem II structure | protein cross-linking

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“…Mutant Strain Generation-The construction of the ⌬psbO strain used in this study has been described previously (26). For the ⌬psb27 mutant, the region surrounding slr1645 (psb27) was amplified from genomic DNA and replacement of the coding region of the gene with a chloramphenicol resistance cassette was achieved by using a fusion PCR technique (supplemental Fig.…”

Section: Methodsmentioning

confidence: 99%

The Psb27 Protein Facilitates Manganese Cluster Assembly in Photosystem II

Roose

Pakrasi

2008

Journal of Biological Chemistry

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112

104

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Photosystem II (PSII) is a large membrane protein complex that uses light energy to convert water to molecular oxygen. This enzyme undergoes an intricate assembly process to ensure accurate and efficient positioning of its many components. It has been proposed that the Psb27 protein, a lumenal extrinsic subunit, serves as a PSII assembly factor. Using a psb27 genetic deletion strain (⌬psb27) of the cyanobacterium Synechocystis sp. PCC 6803, we have defined the role of the Psb27 protein in PSII biogenesis. While the Psb27 protein was not essential for photosynthetic activity, various PSII assembly assays revealed that the ⌬psb27 mutant was defective in integration of the Mn 4 Ca 1 Cl x cluster, the catalytic core of the oxygen-evolving machinery within the PSII complex. The other lumenal extrinsic proteins (PsbO, PsbU, PsbV, and PsbQ) are key components of the fully assembled PSII complex and are important for the water oxidation reaction, but we propose that the Psb27 protein has a distinct function separate from these subunits. We show that the Psb27 protein facilitates Mn 4 Ca 1 Cl x cluster assembly in PSII at least in part by preventing the premature association of the other extrinsic proteins. Thus, we propose an exchange of lumenal subunits and cofactors during PSII assembly, in that the Psb27 protein is replaced by the other extrinsic proteins upon assembly of the Mn 4 Ca 1 Cl x cluster. Furthermore, we show that the Psb27 protein provides a selective advantage for cyanobacterial cells under conditions such as nutrient deprivation where Mn 4 Ca 1 Cl x cluster assembly efficiency is critical for survival.Photosystem II (PSII), 3 a component of the photosynthetic electron transfer chain located in the thylakoid membranes of plants and cyanobacteria, catalyzes the light-driven conversion of water to molecular oxygen. This important reaction connects solar energy to the chemical energy used by the vast majority of life on earth and generates molecular oxygen as a byproduct to sustain the aerobic atmosphere of the planet. PSII is a membrane protein complex comprised of more than 20 protein subunits and numerous cofactors. A number of recent structural studies have increased our understanding of the architecture of the functional complex and provided new insights into the mechanism of this important enzyme (1-4). Briefly, photons initiate the transfer of electrons from a pair of chlorophylls at the reaction center through a series of cofactors to a membrane-soluble quinone. To reset the PSII reaction center, a catalytic center of Mn 4 Ca 1 Cl x removes electrons from water, yielding molecular oxygen.The electron transfer reactions through PSII require precise positioning of its redox active cofactors. Proper assembly of the numerous PSII components is essential, and the PSII biogenesis pathway entails an ordered assembly of the constituent proteins and cofactors (5, 6). Moreover, PSII assembly occurs frequently because this enzyme continually undergoes a cycle of damage and repair. As a consequence of its norma...

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Regulation of Manganese Uptake in Synechocystis 6803 by RfrA, a Member of a Novel Family of Proteins Containing a Repeated Five-Residues Domain

Cited by 30 publications

References 35 publications

Cluster of Genes That Encode Positive and Negative Elements Influencing Filament Length in a Heterocyst-Forming Cyanobacterium

Cluster of Genes That Encode Positive and Negative Elements Influencing Filament Length in a Heterocyst-Forming Cyanobacterium

MS-based cross-linking analysis reveals the location of the PsbQ protein in cyanobacterial photosystem II

The Psb27 Protein Facilitates Manganese Cluster Assembly in Photosystem II

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