• Journal of Life Science
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• v.22 no.8
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• pp.1009-1017
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• 2012

The orf282 gene of Rhodobacter sphaeroides is located between the ccoNOQP operon encoding $cbb_3$ terminal oxidase and the fnrL gene encoding an anaerobic activator, FnrL. Its function remains unknown. In an attempt to reveal the function of the orf282 gene, we disrupted the gene by deleting a portion of the orf282 gene and constructed an orf282-knockout mutant. Two FnrL binding sites were found to be located upstream of orf282, and it was demonstrated that orf282 is positively regulated by FnrL. The orf282 gene is not involved in the regulation of spectral complex formation. The $cbb_3$ oxidase activity detected in the orf282 mutant was comparable to that in the wild-type sample, indicating that the orf282 gene is not involved in the regulation of the ccoNOQP operon and the biosynthesis of the cbb3 cytochrome c oxidase. The elevated promoter activity of the nifH and nifA genes, which are the structural genes of nitrogenase and its regulator, respectively, in the orf282 mutant, suggests that the orf282 gene product acts as a negative effector for nifH and nifA expression.

• Korean Journal of Microbiology
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• v.34 no.3
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• pp.115-119
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• 1998

We cloned the 4.8 kb BglII fragment containing genes downstream pHENX7 from Pseudomonas sp. strain DJ77. The restriction map of the resultant clone, recombinant plasmid pYCS500, was determined. Sequencing analysis of the 465 bp HindIII-ClaI fragment revealed an open reading frame of 282 bp that was then designated phnM. The deduced polypeptide is 93 amino acid residues long with a $M_r$ of 10,008. The PhnM has 37.3-53.9% identity with plant-type ferredoxin proteins such as NahT, XylT, DmpQ, AtdS, PhlG, PhhQ and TbuW and contains the motif similar to well-conserved functional domains of those proteins.

• Proceedings of the Korean Society of Plant Pathology Conference
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• 2003.10a
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• pp.125.3-126
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• 2003

A near full-length sequence of a new tobamovirus infecting Hibiscus rosa-sinensis L. was determined. The genome consists of 58 nucleotides (nt) 5' UTR, followed by a 4.9 kb ORF which methyl transferase helicase domain (128 kDa), readthrough protein RNA dependent RNA polymerase (RdRp) 185 kDa and a 52 kDa protein. The 128 kDa protein had a maximum homology of 51.4 ％ to TMGMV and amino acids (an) were 54.3 ％ identical to TMV- vulgare strain. The 185 kDa RdRp had a maximum homology of 53.5％ to TMV-Ob and KGMMV-Y and a 59.6％ homology at the an level to CGMMV-SH. The MP gene encodes 282 aa and its theoretical molecular weight is 30.4 kDa. The nt and an sequence identities of MP ranged from 38.8％ to 43.9％ and 30.9％ to 37.9％, respectively. The CP gene encodes 163 residues and with a theoretical molecular weight of 18.2 kDa The (nt) and aa sequences of the CP were 46.9 ％ to 51.6％ and 45.3％ to 57.1％ identical to other tobamoviruses, respectively. The predicted virion origin of assembly (OAS) was located in the CP gene. Phylogenetic trees generated based on the nt and as sequences of RdRp, MP and CP genes indicated that this new virus clustered with subgroup II tobamoviruses. Although the CP ORF of this virus shared a high nt and aa sequence identity with Sunn-hemp mosaic virus (SHMV), Western analysis showed that it is serologically unrelated to SHMV. We propose the name Hibiscus virus S (HVS) for this Singapore isolate. This is the first report on a near full-length sequence of a Tobamovirus that infects hibiscus.