Nucleotide and deduced polypeptide sequences of the photosynthetic reaction-center, B870 antenna, and flanking polypeptides from R. capsulata

Youvan, Douglas C.; Bylina, Edward J.; Alberti, Marie; Begusch, Helmut; Hearst, John E.

doi:10.1016/0092-8674(84)90429-x

Cited by 451 publications

(259 citation statements)

References 19 publications

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“…Further scrutiny of the databases revealed two other proteins that contain the same sequence motif: these are the formaldehyde transketolase of Hansenulapolymorpha [11] and the potential product (Rcrcfp) of a hitherto unidentified open reading frame that lies immediately downstream from the gene cluster encoding the photosynthetic reaction centre proteins in R. capsulata [12]. The relevant regions of these proteins too are aligned in fig.…”

Section: Identification Of a Common Sequence Motifmentioning

confidence: 99%

A common structural motif in thiamin pyrophosphate‐binding enzymes

1989

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The amino acid sequences of a wide range of enzymes that utilize thiamin pyrophosphate (TPP) as cofactor have been compared. A common sequence motif approximately 30 residues in length was detected, beginning with the highly conserved sequence -GDG-and concluding with the highly conserved sequence -NN-. Secondary structure predictions suggest that the motif may adopt a flail fold. The same motif was recognised in the primary structure of a protein deduced from the DNA sequence of a hitherto unassigned open reading frame of Rhodobacter capsulata. This putative protein exhibits additional homology with some but not all of the TPP-binding enzymes.

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Section: Identification Of a Common Sequence Motifmentioning

confidence: 99%

A common structural motif in thiamin pyrophosphate‐binding enzymes

1989

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“…These plasmids were constructed by subcloning a 3,412-bp BamHI- pBR322Q1 pCB701 pCB701fl pCB701DfQ pCB7O1EfQ pCB7O1FQl pCB701DfQO pCB701AF pNM480 pNM482 pRPSB104 pRPSB5 PRPSB9 pUC701 pUC9 pUC4-Kixx pZY22 pZY32 pZY33 pZY42 pZY62fl bchB::lacZ'708 crtD233 hsd-J str-2 bchB::lacZ+709 hsd-J str-2 bchB4 crtFJ29 bchE6O4 crtF129 hsd-J str-2 bchH650 crtFl29 hsd-J str- (29). The location of the indicated bch genes involved in BChl biosynthesis is a compilation of previously published data (5,29,35,36 (34) to a density of 50 Klett units. The cells were chilled on ice to 4°C and then harvested by centrifugation at 10,000 x g for 15 min at 4°C.…”

Section: Methodsmentioning

confidence: 99%

Rhodobacter capsulatus genes involved in early steps of the bacteriochlorophyll biosynthetic pathway

1990

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Three open reading frames in the Rhodobacter capsulatus photosynthesis gene cluster, designated FO, F108, and F1025, were disrupted by site-directed mutagenesis. Mutants bearing insertions in these reading frames were defective in converting protoporphyrin IX to magnesium-protoporphyrin monomethyl ester, protochlorophyllide to chlorophyliide a, and magnesium-protoporphyrin monomethyl ester to protochlorophyllide, respectively. These results demonstrate that the genes examined most likely encode enzyme subunits that catalyze steps common to plant and bacterial tetrapyrrole photopigment biosynthetic pathways. The open reading frames were found to be part of a large ll-kilobase operon that encodes numerous genes involved in early steps of the bacteriochlorophyll a biosynthetic pathway.

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“…However, the distribution of other 5' ends, some of which were more prominent than the 5' ends mapping to the 185-bp BstEII-PstI fragment, were not influenced by the BstEIIPstI deletion [compare 5' bands mapping within pufX in ARC6(pAOL12) and ARC6(pARB6; Fig. 3 (27) appears to contain at least some of the loci implicated in the rate-limiting step for degradation of the RC-coding segment of puf mRNA, we examined the consequences of inserting this fragment into the pufB gene, which normally encodes highly stable mRNA sequences. A BalI site was created at the 5' end of pufB by site-directed mutagenesis (plasmid pTXB26; B. Dorge, G. Klug, N. Gad'on, S. N. Cohen, and G. Drews, Biochemistry, in press), and the isolated 185-bp BstEII-PstI fragment was treated with T4 DNA polymerase and then ligated to the BalI ends.…”

Section: Resultsmentioning

confidence: 99%

“…The DNA sequence obtained by Youvan et al (27) predicted the existence of two regions of secondary structure in the mRNA segment downstream of pufX; these were later shown to function as terminators of transcription.…”

Section: Resultsmentioning

confidence: 99%

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Combined actions of multiple hairpin loop structures and sites of rate-limiting endonucleolytic cleavage determine differential degradation rates of individual segments within polycistronic puf operon mRNA

Klug

Cohen

1990

J Bacteriol

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Differential expression of the genes within the puf operon of Rhodobacter capsulatus is accomplished in part by differences in the rate of degradation of different segments of the puf transcript. We report here that decay of puf mRNA sequences specifying the light-harvesting I (LHI) and reaction center (RC) photosynthetic membrane peptides is initiated endoribonucleolytically within a discrete 1.4-kilobase segment of the RC-coding region. Deletion of this segment increased the half-life of the RC-coding region from 8 to 20 min while not affecting decay of LHI-coding sequences upstream from an intercistronic hairpin loop -structure shown previously to impede 3'-to-5' degradation. Prolongation of RC segment half-life was dependent on the presence of other hairpin structures 3' to the RC region. Inserting the endonuclease-sensitive sites into the LHI-coding segment markedly accelerated its degradation. Our results suggest that differential degradation of the RC-and LHI-coding segments of puf mRNA is accomplished at least in part by the combined actions of RC region-specific endonuclease(s), one or more exonucleases, and several strategically located exonucleaseimpeding hairpins.

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Nucleotide and deduced polypeptide sequences of the photosynthetic reaction-center, B870 antenna, and flanking polypeptides from R. capsulata

Cited by 451 publications

References 19 publications

A common structural motif in thiamin pyrophosphate‐binding enzymes

A common structural motif in thiamin pyrophosphate‐binding enzymes

Rhodobacter capsulatus genes involved in early steps of the bacteriochlorophyll biosynthetic pathway

Combined actions of multiple hairpin loop structures and sites of rate-limiting endonucleolytic cleavage determine differential degradation rates of individual segments within polycistronic puf operon mRNA

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