| 21 matches found in 5 documents. Search time: 0.082 seconds. |
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Score: 11.00 |
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| Title: Solution structure of the DNA binding domain of rice telomere binding protein RTBP1 .
| | Author: Ko S Yu EY Shin J Yoo HH Tanaka T Kim WT Cho HS Lee W Chung IK | | Journal: Biochemistry Citation: V : 48 P : 827-38 Year: 2009 Type: MEDLINE | | Literature: oryza Field: abstract Doc ID: pub19152316 Accession (PMID): 19152316 | | Abstract: RTBP1 is a rice telomeric protein that binds to the duplex array of TTTAGGG repeats at chromosome ends .
The DNA binding domain of RTBP1 contains a Myb-type DNA binding motif and a highly conserved C-terminal Myb extension that is unique to plant telomeric proteins .
Using an electrophoretic mobility shift assay , we identified the C-terminal 110-amino acid region ( RTBP1 ( 506-615 ) ) as the minimal telomeric DNA binding domain , suggesting that the Myb extension is required for binding plant telomeric DNA .
Like other telomeric proteins such as human TRF1 and yeast Rap1 , RTBP1 induced a DNA bending in the telomeric repeat sequence , suggesting that RTBP1 may play a role in establishing and/or maintaining an active telomere configuration in vivo .
To elucidate the DNA binding mode of RTBP1 , we determined the three-dimensional structure of RTBP1 ( 506-615 ) in solution by NMR spectroscopy .
The overall structure of RTBP1 ( 506-615 ) is composed of four alpha-helices and stabilized by three hydrophobic patches .
The second and third helices in RTBP1 form a helix-turn-helix motif that interacts directly with DNA .
The fourth helix located in the Myb extension is essential for binding to telomeric DNA via stabilization of the overall structure of the RTBP1 DNA binding domain .
When DNA bound to RTBP1 ( 506-615 ) , large chemical shift perturbations were induced in the N-terminal arm , helix 3 , and the loop between helices 3 and 4 .
These results suggest that helix 3 functions as a sequence-specific recognition helix while the N-terminal arm stabilizes the DNA binding .
| Matching Sentences:
[ Sen. 4, subscore: 2.00 ]: Like other telomeric proteins such as human TRF1 and yeast Rap1 , RTBP1 induced a DNA bending in the telomeric repeat sequence , suggesting that RTBP1 may play a role in establishing and/or maintaining an active telomere configuration in vivo .
[ Sen. 5, subscore: 2.00 ]: To elucidate the DNA binding mode of RTBP1 , we determined the three-dimensional structure of RTBP1 ( 506-615 ) in solution by NMR spectroscopy .
[ Sen. 1, subscore: 1.00 ]: RTBP1 is a rice telomeric protein that binds to the duplex array of TTTAGGG repeats at chromosome ends .
[ Sen. 2, subscore: 1.00 ]: The DNA binding domain of RTBP1 contains a Myb-type DNA binding motif and a highly conserved C-terminal Myb extension that is unique to plant telomeric proteins .
[ Sen. 3, subscore: 1.00 ]: Using an electrophoretic mobility shift assay , we identified the C-terminal 110-amino acid region ( RTBP1 ( 506-615 ) ) as the minimal telomeric DNA binding domain , suggesting that the Myb extension is required for binding plant telomeric DNA .
[ Sen. 6, subscore: 1.00 ]: The overall structure of RTBP1 ( 506-615 ) is composed of four alpha-helices and stabilized by three hydrophobic patches .
[ Sen. 7, subscore: 1.00 ]: The second and third helices in RTBP1 form a helix-turn-helix motif that interacts directly with DNA .
[ Sen. 8, subscore: 1.00 ]: The fourth helix located in the Myb extension is essential for binding to telomeric DNA via stabilization of the overall structure of the RTBP1 DNA binding domain .
[ Sen. 9, subscore: 1.00 ]: When DNA bound to RTBP1 ( 506-615 ) , large chemical shift perturbations were induced in the N-terminal arm , helix 3 , and the loop between helices 3 and 4 .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 8.00 |
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| Title: Sequence-specific DNA recognition by the Myb-like domain of plant telomeric protein RTBP1 .
| | Author: Yu EY Kim SE Kim JH Ko JH Cho MH Chung IK .
| | Journal: J Biol . Chem . Citation: V : 275 ( 31 ) P : 24208-14 Year: 2000 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10811811 Accession (PMID): 10811811 | | Abstract: We have identified a rice gene encoding a DNA-binding protein that specifically recognizes the telomeric repeat sequence TTTAGGG found in plants .
This gene , which we refer to as RTBP1 ( rice telomere-binding protein 1 ) , encodes a polypeptide with a predicted molecular mass of 70 kDa .
RTBP1 is ubiquitously expressed in various organs and binds DNA with two or more duplex TTTAGGG repeats .
The predicted protein sequence includes a single domain at the C terminus with extensive homology to Myb-like DNA binding motif .
The Myb-like domain of RTBP1 is very closely related to that of other telomere-binding proteins , including TRF1 , TRF2 , Taz1p , and Tbf1p , indicating that DNA-binding domains of telomere-binding proteins are well conserved among evolutionarily distant species .
To obtain precise information on the sequence of the DNA binding site recognized by RTBP1 , we analyzed the sequence-specific binding properties of the isolated Myb-like domain of RTBP1 .
The isolated Myb-like domain was capable of sequence-specific DNA binding as a homodimer .
Gel retardation analysis with a series of mutated telomere probes revealed that the internal GGGTTT sequence in the two-telomere repeats is critical for binding of Myb-like domain of RTBP1 , which is consistent with the model of the TRF1 . DNA complex showing that base-specific contacts are made within the sequence GGGTTA .
To the best of our knowledge , RTBP1 is the first cloned gene in which the product is able to bind double-stranded telomeric DNA in plants .
Because the Myb-like domain appears to be a significant motif for a large class of proteins that bind the duplex telomeric DNA , RTBP1 may play important roles in plant telomere function in vivo . | Matching Sentences:
[ Sen. 6, subscore: 2.00 ]: To obtain precise information on the sequence of the DNA binding site recognized by RTBP1 , we analyzed the sequence-specific binding properties of the isolated Myb-like domain of RTBP1 .
[ Sen. 2, subscore: 1.00 ]: This gene , which we refer to as RTBP1 ( rice telomere-binding protein 1 ) , encodes a polypeptide with a predicted molecular mass of 70 kDa .
[ Sen. 3, subscore: 1.00 ]: RTBP1 is ubiquitously expressed in various organs and binds DNA with two or more duplex TTTAGGG repeats .
[ Sen. 5, subscore: 1.00 ]: The Myb-like domain of RTBP1 is very closely related to that of other telomere-binding proteins , including TRF1 , TRF2 , Taz1p , and Tbf1p , indicating that DNA-binding domains of telomere-binding proteins are well conserved among evolutionarily distant species .
[ Sen. 8, subscore: 1.00 ]: Gel retardation analysis with a series of mutated telomere probes revealed that the internal GGGTTT sequence in the two-telomere repeats is critical for binding of Myb-like domain of RTBP1 , which is consistent with the model of the TRF1 . DNA complex showing that base-specific contacts are made within the sequence GGGTTA .
[ Sen. 9, subscore: 1.00 ]: To the best of our knowledge , RTBP1 is the first cloned gene in which the product is able to bind double-stranded telomeric DNA in plants .
[ Sen. 10, subscore: 1.00 ]: Because the Myb-like domain appears to be a significant motif for a large class of proteins that bind the duplex telomeric DNA , RTBP1 may play important roles in plant telomere function in vivo .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 5.00 |
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| Title: Suppression of RICE TELOMERE BINDING PROTEIN 1 results in severe and gradual developmental defects accompanied by genome instability in rice .
| | Author: Hong JP Byun MY Koo DH An K Bang JW Chung IK An G Kim WT | | Journal: Plant Cell Citation: V : 19 P : 1770-81 Year: 2007 Type: MEDLINE | | Literature: oryza Field: abstract Doc ID: pub17586654 Accession (PMID): 17586654 | | Abstract: Although several potential telomere binding proteins have been identified in higher plants , their in vivo functions are still unknown at the plant level .
Both knockout and antisense mutants of RICE TELOMERE BINDING PROTEIN1 ( RTBP1 ) exhibited markedly longer telomeres relative to those of the wild type , indicating that the amount of functional RTBP1 is inversely correlated with telomere length . rtbp1 plants displayed progressive and severe developmental abnormalities in both germination and postgermination growth of vegetative organs over four generations ( G1 to G4 ) .
Reproductive organ formation , including panicles , stamens , and spikelets , was also gradually and severely impaired in G1 to G4 mutants .
Up to 11 . 4 , 17 . 2 , and 26 . 7% of anaphases in G2 , G3 , and G4 mutant pollen mother cells , respectively , exhibited one or more chromosomal fusions , and this progressively increasing aberrant morphology was correlated with an increased frequency of anaphase bridges containing telomeric repeat DNA .
Furthermore , 35S : anti-RTBP1 plants expressing lower levels of RTBP1 mRNA exhibited developmental phenotypes intermediate between the wild type and mutants in all aspects examined , including telomere length , vegetative and reproductive growth , and degree of genomic anomaly .
These results suggest that RTBP1 plays dual roles in rice ( Oryza sativa ) , as both a negative regulator of telomere length and one of positive and functional components for proper architecture of telomeres .
| Matching Sentences:
[ Sen. 2, subscore: 3.00 ]: Both knockout and antisense mutants of RICE TELOMERE BINDING PROTEIN1 ( RTBP1 ) exhibited markedly longer telomeres relative to those of the wild type , indicating that the amount of functional RTBP1 is inversely correlated with telomere length . rtbp1 plants displayed progressive and severe developmental abnormalities in both germination and postgermination growth of vegetative organs over four generations ( G1 to G4 ) .
[ Sen. 5, subscore: 1.00 ]: Furthermore , 35S : anti-RTBP1 plants expressing lower levels of RTBP1 mRNA exhibited developmental phenotypes intermediate between the wild type and mutants in all aspects examined , including telomere length , vegetative and reproductive growth , and degree of genomic anomaly .
[ Sen. 6, subscore: 1.00 ]: These results suggest that RTBP1 plays dual roles in rice ( Oryza sativa ) , as both a negative regulator of telomere length and one of positive and functional components for proper architecture of telomeres .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 1.00 |
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| Title: Sequence-specific DNA recognition by the Myb-like domain of plant telomeric protein RTBP1 .
| | Author: Yu EY Kim SE Kim JH Ko JH Cho MH Chung IK .
| | Journal: J Biol . Chem . Citation: V : 275 ( 31 ) P : 24208-14 Year: 2000 Type: ARTICLE | | Literature: oryza Field: title Doc ID: pub10811811 Accession (PMID): 10811811 | | Abstract: We have identified a rice gene encoding a DNA-binding protein that specifically recognizes the telomeric repeat sequence TTTAGGG found in plants .
This gene , which we refer to as RTBP1 ( rice telomere-binding protein 1 ) , encodes a polypeptide with a predicted molecular mass of 70 kDa .
RTBP1 is ubiquitously expressed in various organs and binds DNA with two or more duplex TTTAGGG repeats .
The predicted protein sequence includes a single domain at the C terminus with extensive homology to Myb-like DNA binding motif .
The Myb-like domain of RTBP1 is very closely related to that of other telomere-binding proteins , including TRF1 , TRF2 , Taz1p , and Tbf1p , indicating that DNA-binding domains of telomere-binding proteins are well conserved among evolutionarily distant species .
To obtain precise information on the sequence of the DNA binding site recognized by RTBP1 , we analyzed the sequence-specific binding properties of the isolated Myb-like domain of RTBP1 .
The isolated Myb-like domain was capable of sequence-specific DNA binding as a homodimer .
Gel retardation analysis with a series of mutated telomere probes revealed that the internal GGGTTT sequence in the two-telomere repeats is critical for binding of Myb-like domain of RTBP1 , which is consistent with the model of the TRF1 . DNA complex showing that base-specific contacts are made within the sequence GGGTTA .
To the best of our knowledge , RTBP1 is the first cloned gene in which the product is able to bind double-stranded telomeric DNA in plants .
Because the Myb-like domain appears to be a significant motif for a large class of proteins that bind the duplex telomeric DNA , RTBP1 may play important roles in plant telomere function in vivo . | Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: Sequence-specific DNA recognition by the Myb-like domain of plant telomeric protein RTBP1 .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 1.00 |
|---|
| Title: Solution structure of the DNA binding domain of rice telomere binding protein RTBP1 .
| | Author: Ko S Yu EY Shin J Yoo HH Tanaka T Kim WT Cho HS Lee W Chung IK | | Journal: Biochemistry Citation: V : 48 P : 827-38 Year: 2009 Type: MEDLINE | | Literature: oryza Field: title Doc ID: pub19152316 Accession (PMID): 19152316 | | Abstract: RTBP1 is a rice telomeric protein that binds to the duplex array of TTTAGGG repeats at chromosome ends .
The DNA binding domain of RTBP1 contains a Myb-type DNA binding motif and a highly conserved C-terminal Myb extension that is unique to plant telomeric proteins .
Using an electrophoretic mobility shift assay , we identified the C-terminal 110-amino acid region ( RTBP1 ( 506-615 ) ) as the minimal telomeric DNA binding domain , suggesting that the Myb extension is required for binding plant telomeric DNA .
Like other telomeric proteins such as human TRF1 and yeast Rap1 , RTBP1 induced a DNA bending in the telomeric repeat sequence , suggesting that RTBP1 may play a role in establishing and/or maintaining an active telomere configuration in vivo .
To elucidate the DNA binding mode of RTBP1 , we determined the three-dimensional structure of RTBP1 ( 506-615 ) in solution by NMR spectroscopy .
The overall structure of RTBP1 ( 506-615 ) is composed of four alpha-helices and stabilized by three hydrophobic patches .
The second and third helices in RTBP1 form a helix-turn-helix motif that interacts directly with DNA .
The fourth helix located in the Myb extension is essential for binding to telomeric DNA via stabilization of the overall structure of the RTBP1 DNA binding domain .
When DNA bound to RTBP1 ( 506-615 ) , large chemical shift perturbations were induced in the N-terminal arm , helix 3 , and the loop between helices 3 and 4 .
These results suggest that helix 3 functions as a sequence-specific recognition helix while the N-terminal arm stabilizes the DNA binding .
| Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: Solution structure of the DNA binding domain of rice telomere binding protein RTBP1 .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
