The large subunit of ribulose-1,5-bisphosphate carboxylase-oxygenase is encoded in the inverted repeat sequence of the Chlamydomonas eugametos chloroplast genome

1985 ◽  
Vol 9 (2) ◽  
pp. 139-145 ◽  
Author(s):  
Claude Lemieux ◽  
Monique Turmel ◽  
Verner L. Seligy ◽  
Robert W. Lee
Keyword(s):  
Chloroplast Genome ◽  
Inverted Repeat ◽  
Large Subunit ◽  
Repeat Sequence ◽  
Inverted Repeat Sequence ◽  
Bisphosphate Carboxylase ◽  
Chlamydomonas Eugametos

scholarly journals Formation of Large Palindromic DNA by Homologous Recombination of Short Inverted Repeat Sequences in Saccharomyces cerevisiae

Genetics ◽  
2002 ◽  
Vol 161 (3) ◽  
pp. 1065-1075
Author(s):  
David K Butler ◽  
David Gillespie ◽  
Brandi Steele
Keyword(s):  
Homologous Recombination ◽  
Inverted Repeat ◽  
Excision Repair ◽  
Strand Break ◽  
Double Strand Break ◽  
Repeat Sequence ◽  
Inverted Repeat Sequence ◽  
Repeat Sequences ◽  
Dna Double Strand Break ◽  
Intermolecular Reaction

Abstract Large DNA palindromes form sporadically in many eukaryotic and prokaryotic genomes and are often associated with amplified genes. The presence of a short inverted repeat sequence near a DNA double-strand break has been implicated in the formation of large palindromes in a variety of organisms. Previously we have established that in Saccharomyces cerevisae a linear DNA palindrome is efficiently formed from a single-copy circular plasmid when a DNA double-strand break is introduced next to a short inverted repeat sequence. In this study we address whether the linear palindromes form by an intermolecular reaction (that is, a reaction between two identical fragments in a head-to-head arrangement) or by an unusual intramolecular reaction, as it apparently does in other examples of palindrome formation. Our evidence supports a model in which palindromes are primarily formed by an intermolecular reaction involving homologous recombination of short inverted repeat sequences. We have also extended our investigation into the requirement for DNA double-strand break repair genes in palindrome formation. We have found that a deletion of the RAD52 gene significantly reduces palindrome formation by intermolecular recombination and that deletions of two other genes in the RAD52-epistasis group (RAD51 and MRE11) have little or no effect on palindrome formation. In addition, palindrome formation is dramatically reduced by a deletion of the nucleotide excision repair gene RAD1.

scholarly journals The yjeB (nsrR) Gene of Escherichia coli Encodes a Nitric Oxide-Sensitive Transcriptional Regulator

2006 ◽  
Vol 188 (3) ◽  
pp. 874-881 ◽  
Author(s):  
Diane M. Bodenmiller ◽  
Stephen Spiro
Keyword(s):  
Nitric Oxide ◽  
Escherichia Coli ◽  
Inverted Repeat ◽  
Nitrosative Stress ◽  
Protein A ◽  
Repeat Sequence ◽  
Negative Regulator ◽  
Inverted Repeat Sequence ◽  
Multiple Copies ◽  
Regulatory Model

ABSTRACT Microarray studies of the Escherichia coli response to nitric oxide and nitrosative stress have suggested that additional transcriptional regulators of this response remain to be characterized. We identify here the product of the yjeB gene as a negative regulator of the transcription of the ytfE, hmpA and ygbA genes, all of which are known to be upregulated by nitrosative stress. Transcriptional fusions to the promoters of these genes were expressed constitutively in a yjeB mutant, indicating that all three are targets for repression by YjeB. An inverted repeat sequence that overlaps the −10 element of all three promoters is proposed to be a binding site for the YjeB protein. A similar inverted repeat sequence was identified in the tehA promoter, which is also known to be sensitive to nitrosative stress. The ytfE, hmpA, ygbA, and tehA promoters all caused derepression of a ytfE-lacZ transcriptional fusion when present in the cell in multiple copies, presumably by a repressor titration effect, suggesting the presence of functional YjeB binding sites in these promoters. However, YjeB regulation of tehA was weak, as judged by the activity of a tehA-lacZ fusion, perhaps because YjeB repression of tehA is masked by other regulatory mechanisms. Promoters regulated by YjeB could be derepressed by iron limitation, which is consistent with an iron requirement for YjeB activity. The YjeB protein is a member of the Rrf2 family of transcriptional repressors and shares three conserved cysteine residues with its closest relatives. We propose a regulatory model in which the YjeB repressor is directly sensitive to nitrosative stress. On the basis of similarity to the nitrite-responsive repressor NsrR from Nitrosomonas europaea, we propose that the yjeB gene of E. coli be renamed nsrR.

A Novel Unusual DNA Structure Formed in an Inverted Repeat Sequence

1998 ◽  
Vol 246 (2) ◽  
pp. 532-534 ◽  
Author(s):  
Mikio Kato ◽  
Kyouko Matsunaga ◽  
Nobuyoshi Shimizu
Keyword(s):  
Inverted Repeat ◽  
Dna Structure ◽  
Repeat Sequence ◽  
Inverted Repeat Sequence

scholarly journals Geobacter uraniireducens NikR Displays a DNA Binding Mode Distinct from Other Members of the NikR Family

2010 ◽  
Vol 192 (17) ◽  
pp. 4327-4336 ◽  
Author(s):  
Erin L. Benanti ◽  
Peter T. Chivers
Keyword(s):  
Dna Binding ◽  
Inverted Repeat ◽  
Dna Recognition ◽  
Binding Mode ◽  
Repeat Sequence ◽  
Amino Acid Sequences ◽  
Inverted Repeat Sequence ◽  
Promoter Regions ◽  
Β Sheets ◽  
Β Sheet

ABSTRACT NikR is a nickel-responsive ribbon-helix-helix transcription factor present in many bacteria and archaea. The DNA binding properties of Escherichia coli and Helicobacter pylori NikR (factors EcNikR and HpNikR, respectively) have revealed variable features of DNA recognition. EcNikR represses a single operon by binding to a perfect inverted repeat sequence, whereas HpNikR binds to promoters from multiple genes that contain poorly conserved inverted repeats. These differences are due in large part to variations in the amino acid sequences of the DNA-contacting β-sheets, as well as residues preceding the β-sheets of these two proteins. We present here evidence of another variation in DNA recognition by the NikR protein from Geobacter uraniireducens (GuNikR). GuNikR has an Arg-Gly-Ser β-sheet that binds specifically to an inverted repeat sequence distinct from those recognized by Ec- or HpNikR. The N-terminal residues that precede the GuNikR β-sheet residues are required for high-affinity DNA binding. Mutation of individual arm residues dramatically reduced the affinity of GuNikR for specific DNA. Interestingly, GuNikR tetramers are capable of binding cooperatively to the promoter regions of two different genes, nik(MN)1 and nik(MN)2. Cooperativity was not observed for the closely related G. bemidjiensis NikR, which recognizes the same operator sequence. The cooperative mode of DNA binding displayed by GuNikR could affect the sensitivity of transporter gene expression to changes in intracellular nickel levels.

scholarly journals A highly conserved, 5′ untranslated, inverted repeat sequence is ineffective in translational control of the α1(I) collagen gene

1988 ◽  
Vol 16 (23) ◽  
pp. 11398-11399
Author(s):  
Paul Bornstein ◽  
John Mckay ◽  
Sreelekha Devarayalu ◽  
Susan C. Cook
Keyword(s):  
Translational Control ◽  
Inverted Repeat ◽  
Repeat Sequence ◽  
Collagen Gene ◽  
Inverted Repeat Sequence
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