trnR-CCG is not unique to the plastid DNA of the liverwortMarchantia: gene identification from the mossPhyscomitrella patens

Kasten, B.; Wehe, M.; Reski, Ralf; Abel, W. O.

doi:10.1093/nar/19.18.5074

Cited by 12 publications

(9 citation statements)

References 8 publications

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“…Anticodon loop sequence of P. patens tRNA Arg -ACG The P. patens plastid genome contains three distinct arginine tRNA genes, trnR-CCG, trnR-ACG, and trnR-UCU (Sugiura et al, 2003). trnR-CCG is located between rbcL and accD in P. patens and a typical clover-leaf structure can form with a pair of mismatching nucleotides (T6AET68) in the aminoacyl stem (Kasten et al, 1991). The CGG codon decoded by trnR-CCG appears in only 1.7% of the total 1019 arginine codons in 83 protein genes and occurs in only 15 protein-coding genes in P. patens plastids.…”

Section: Resultsmentioning

confidence: 99%

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Plastid transformation reveals that moss tRNA^Arg‐CCG is not essential for plastid function

Sugiura

Sugita²

2004

The Plant Journal

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SummaryThree distinct arginine tRNA genes, trnR-CCG, trnR-ACG, and trnR-UCU, are present in the plastid genome of bryophytes, whereas only the latter two trnR genes are present in the major vascular plants, except for black pine. trnR-CCG is located between rbcL and accD in the moss Physcomitrella patens and it was previously believed to be functional in plastids. However, no trnR-CCG transcript has been detected by Northern hybridization, and the codon usage of CGG is quite low in plastid protein-coding sequences. This raises the possibility that trnR-CCG is non-functional. To investigate this possibility, we integrated a foreign gene into the trnR-CCG coding region via homologous recombination, and constructed stable plastid trnR-CCG knockout moss transformants. The trnR-CCG knock-out transformants grew normally, indicating that the P. patens trnR-CCG gene is not essential for plastid function.

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Section: Resultsmentioning

confidence: 99%

“…, 2003). trnR‐CCG is located between rbcL and accD in P. patens and a typical clover‐leaf structure can form with a pair of mismatching nucleotides (T6·T68) in the aminoacyl stem (Kasten et al. , 1991).…”

Section: Anticodon Loop Sequence Of P Patens Trnaarg‐acgmentioning

confidence: 99%

Plastid transformation reveals that moss tRNA^Arg‐CCG is not essential for plastid function

Sugiura

Sugita²

2004

The Plant Journal

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“…However, so far, little is known at the molecular level in Physcomitrel/a. Some sequences have been determined in this lab, including the first mitochondrial DNA sequence from an archegoniate (cox3; Marienfeld et al, 1991) and the only plastid DNA sequences from a moss (Kasten et al, 1991;Kasten et al, 1992;Kruse et al, 1995). The sequence of about ten nuclear encoded genes and cDNAs have also been determined (for a review: Reski, 1998).…”

Section: Introductionmentioning

confidence: 99%

Moss (Physcomitrella patens) Expressed Sequence Tags Include Several Sequences which are Novel for Plants*

Reski

Reynolds

Wehe³

et al. 1998

Botanica Acta

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The moss Physcomitrella patens (Hedw.) B.S.G. is the first land plant in which gene disruption by homologous recombination is directly accessible. In order to obtain cloned sequences which may be used in such an approach, complementary DNAs (cDNAs) have been isolated by subtractive hybridisation of representative cDNA libraries from cytokinin-treated tissue. Sequencing of these clones from both ends yielded over 35 kb of non-redundant sequence information, of which 20 kb results from clones which appear to be novel to plants. Database comparisons have revealed that 39 of the expressed sequence tags (ESTs) generated show significant homology to identified sequences. Analysis of these ESTs shows a high degree of conservation between Physcomitrella and seed plant sequences, and codon usage is found to be very similar to that in dicotyledonous species. Furthermore, 43 sequences showing no significant homology to sequences in the databases represent previously unidentified expressed genes.

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“…In 1992 the sequencing of the accD gene, encoding the βsubunit of the carboxyltransferase (βCT) subunit of the E. coli ACCase [13], enabled a putative function to be assigned to an open reading frame (ORF) reported in the chloroplast genome of several plant species. The ORFs included pea [31,32], tobacco [33], the parasitic plants Cuscuta reflexa (G. Haberhausen ; EMBL accession number X69803) and Epifagus irginiana [34], Pinus thunbergii [35], Marchantia polymorpha [36], Physcomitrella patens [37] and Angiopteris lygodiifolia [38]. Despite the knowledge of these homologous ORFs, much less was known about their expression and the association between their predicted products and ACCase activity.…”

Section: Introductionmentioning

confidence: 99%

Biotin carboxyl carrier protein and carboxyltransferase subunits of the multi-subunit form of acetyl-CoA carboxylase from Brassica napus: cloning and analysis of expression during oilseed rape embryogenesis

Elborough

Winz

Deka

et al. 1996

Biochemical Journal

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In the oilseed rape Brassica napus there are two forms of acetyl-CoA carboxylase (ACCase). As in other dicotyledonous plants there is a type I ACCase, the single polypeptide 220 kDa form, and a type II multi-subunit complex analogous to that of Escherichia coli and Anabaena. This paper describes the cloning and characterization of a plant biotin carboxyl carrier protein (BCCP) from the type II ACCase complex that shows 61% identity/79% similarity with Anabaena BCCP at the amino acid level. Six classes of nuclear encoded oilseed rape BCCP cDNA were clones, two of which contained the entire coding region. The BCCP sequences allowed the assignment of function to two previously unassigned Arabidopsis expressed sequence tag (EST) sequences. We also report the cloning of a second type II ACCase component from oilseed rape, the beta-carboxyltransferase subunit (betaCT), which is chloroplast-encoded. Northern analysis showed that although the relative levels of BCCP and betaCT mRNA differed between different oilseed rape tissues, their temporal patterns of expression were identical during embryo development. At the protein level, expression of BCCP during embryo development was studied by Western blotting, using affinity-purified anti-biotin polyclonal sera. With this technique a 35 kDa protein thought to be BCCP was shown to reside within the chloroplast. This analysis also permitted us to view the differential expression of several unidentified biotinylated proteins during embryogenesis.

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trnR-CCG is not unique to the plastid DNA of the liverwortMarchantia: gene identification from the mossPhyscomitrella patens

Cited by 12 publications

References 8 publications

Plastid transformation reveals that moss tRNA^Arg‐CCG is not essential for plastid function

Plastid transformation reveals that moss tRNA^Arg‐CCG is not essential for plastid function

Moss (Physcomitrella patens) Expressed Sequence Tags Include Several Sequences which are Novel for Plants*

Biotin carboxyl carrier protein and carboxyltransferase subunits of the multi-subunit form of acetyl-CoA carboxylase from Brassica napus: cloning and analysis of expression during oilseed rape embryogenesis

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trnR-CCG is not unique to the plastid DNA of the liverwortMarchantia: gene identification from the mossPhyscomitrella patens

Cited by 12 publications

References 8 publications

Plastid transformation reveals that moss tRNAArg‐CCG is not essential for plastid function

Plastid transformation reveals that moss tRNAArg‐CCG is not essential for plastid function

Moss (Physcomitrella patens) Expressed Sequence Tags Include Several Sequences which are Novel for Plants*

Biotin carboxyl carrier protein and carboxyltransferase subunits of the multi-subunit form of acetyl-CoA carboxylase from Brassica napus: cloning and analysis of expression during oilseed rape embryogenesis

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Plastid transformation reveals that moss tRNA^Arg‐CCG is not essential for plastid function

Plastid transformation reveals that moss tRNA^Arg‐CCG is not essential for plastid function