author_facet Kato, H
Nagamine, M
Kominami, R
Muramatsu, M
Kato, H
Nagamine, M
Kominami, R
Muramatsu, M
author Kato, H
Nagamine, M
Kominami, R
Muramatsu, M
spellingShingle Kato, H
Nagamine, M
Kominami, R
Muramatsu, M
Molecular and Cellular Biology
Formation of the transcription initiation complex on mammalian rDNA.
Cell Biology
Molecular Biology
author_sort kato, h
spelling Kato, H Nagamine, M Kominami, R Muramatsu, M 0270-7306 1098-5549 Informa UK Limited Cell Biology Molecular Biology http://dx.doi.org/10.1128/mcb.6.10.3418 <jats:p>Steps for the formation of transcription initiation complex on the human rRNA gene (rDNA) in vitro were analyzed with partially purified transcription factors and RNA polymerase I. The reaction requires at least two factors besides RNA polymerase I for maximal efficiency. Preincubation and short-pulse analyses of the accurate transcripts revealed the following steps. First, the species-dependent factor, designated TFID, bound to the rDNA template, forming a preinitiation complex (PIC-1) which was resistant to a moderate concentration (0.015 to 0.02%) of Sarkosyl. Other factors, designated TFIA and RNA polymerase I, were then added to convert it to the final preinitiation complex PIC-3. This complex incorporated the first two nucleoside triphosphates of the starting site to complete the initiation complex (IC), which was resistant to a high concentration (0.2%) of Sarkosyl. Binding of TFID was rate limiting in the overall initiation reaction in vitro. Together with the kinetics of incorporation, the results are interpreted to mean that TFID, one bound, remains complexed with rDNA together with TFIA as the PIC-2 for many rounds of transcription by RNA polymerase I. Thus, the formation of PIC-2 may be a prerequisite for the stable opening of rDNA for transcription in vivo.</jats:p> Formation of the transcription initiation complex on mammalian rDNA. Molecular and Cellular Biology
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match_str kato1986formationofthetranscriptioninitiationcomplexonmammalianrdna
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series Molecular and Cellular Biology
source_id 49
title Formation of the transcription initiation complex on mammalian rDNA.
title_unstemmed Formation of the transcription initiation complex on mammalian rDNA.
title_full Formation of the transcription initiation complex on mammalian rDNA.
title_fullStr Formation of the transcription initiation complex on mammalian rDNA.
title_full_unstemmed Formation of the transcription initiation complex on mammalian rDNA.
title_short Formation of the transcription initiation complex on mammalian rDNA.
title_sort formation of the transcription initiation complex on mammalian rdna.
topic Cell Biology
Molecular Biology
url http://dx.doi.org/10.1128/mcb.6.10.3418
publishDate 1986
physical 3418-3427
description <jats:p>Steps for the formation of transcription initiation complex on the human rRNA gene (rDNA) in vitro were analyzed with partially purified transcription factors and RNA polymerase I. The reaction requires at least two factors besides RNA polymerase I for maximal efficiency. Preincubation and short-pulse analyses of the accurate transcripts revealed the following steps. First, the species-dependent factor, designated TFID, bound to the rDNA template, forming a preinitiation complex (PIC-1) which was resistant to a moderate concentration (0.015 to 0.02%) of Sarkosyl. Other factors, designated TFIA and RNA polymerase I, were then added to convert it to the final preinitiation complex PIC-3. This complex incorporated the first two nucleoside triphosphates of the starting site to complete the initiation complex (IC), which was resistant to a high concentration (0.2%) of Sarkosyl. Binding of TFID was rate limiting in the overall initiation reaction in vitro. Together with the kinetics of incorporation, the results are interpreted to mean that TFID, one bound, remains complexed with rDNA together with TFIA as the PIC-2 for many rounds of transcription by RNA polymerase I. Thus, the formation of PIC-2 may be a prerequisite for the stable opening of rDNA for transcription in vivo.</jats:p>
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author Kato, H, Nagamine, M, Kominami, R, Muramatsu, M
author_facet Kato, H, Nagamine, M, Kominami, R, Muramatsu, M, Kato, H, Nagamine, M, Kominami, R, Muramatsu, M
author_sort kato, h
container_issue 10
container_start_page 3418
container_title Molecular and Cellular Biology
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description <jats:p>Steps for the formation of transcription initiation complex on the human rRNA gene (rDNA) in vitro were analyzed with partially purified transcription factors and RNA polymerase I. The reaction requires at least two factors besides RNA polymerase I for maximal efficiency. Preincubation and short-pulse analyses of the accurate transcripts revealed the following steps. First, the species-dependent factor, designated TFID, bound to the rDNA template, forming a preinitiation complex (PIC-1) which was resistant to a moderate concentration (0.015 to 0.02%) of Sarkosyl. Other factors, designated TFIA and RNA polymerase I, were then added to convert it to the final preinitiation complex PIC-3. This complex incorporated the first two nucleoside triphosphates of the starting site to complete the initiation complex (IC), which was resistant to a high concentration (0.2%) of Sarkosyl. Binding of TFID was rate limiting in the overall initiation reaction in vitro. Together with the kinetics of incorporation, the results are interpreted to mean that TFID, one bound, remains complexed with rDNA together with TFIA as the PIC-2 for many rounds of transcription by RNA polymerase I. Thus, the formation of PIC-2 may be a prerequisite for the stable opening of rDNA for transcription in vivo.</jats:p>
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id ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTEyOC9tY2IuNi4xMC4zNDE4
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spelling Kato, H Nagamine, M Kominami, R Muramatsu, M 0270-7306 1098-5549 Informa UK Limited Cell Biology Molecular Biology http://dx.doi.org/10.1128/mcb.6.10.3418 <jats:p>Steps for the formation of transcription initiation complex on the human rRNA gene (rDNA) in vitro were analyzed with partially purified transcription factors and RNA polymerase I. The reaction requires at least two factors besides RNA polymerase I for maximal efficiency. Preincubation and short-pulse analyses of the accurate transcripts revealed the following steps. First, the species-dependent factor, designated TFID, bound to the rDNA template, forming a preinitiation complex (PIC-1) which was resistant to a moderate concentration (0.015 to 0.02%) of Sarkosyl. Other factors, designated TFIA and RNA polymerase I, were then added to convert it to the final preinitiation complex PIC-3. This complex incorporated the first two nucleoside triphosphates of the starting site to complete the initiation complex (IC), which was resistant to a high concentration (0.2%) of Sarkosyl. Binding of TFID was rate limiting in the overall initiation reaction in vitro. Together with the kinetics of incorporation, the results are interpreted to mean that TFID, one bound, remains complexed with rDNA together with TFIA as the PIC-2 for many rounds of transcription by RNA polymerase I. Thus, the formation of PIC-2 may be a prerequisite for the stable opening of rDNA for transcription in vivo.</jats:p> Formation of the transcription initiation complex on mammalian rDNA. Molecular and Cellular Biology
spellingShingle Kato, H, Nagamine, M, Kominami, R, Muramatsu, M, Molecular and Cellular Biology, Formation of the transcription initiation complex on mammalian rDNA., Cell Biology, Molecular Biology
title Formation of the transcription initiation complex on mammalian rDNA.
title_full Formation of the transcription initiation complex on mammalian rDNA.
title_fullStr Formation of the transcription initiation complex on mammalian rDNA.
title_full_unstemmed Formation of the transcription initiation complex on mammalian rDNA.
title_short Formation of the transcription initiation complex on mammalian rDNA.
title_sort formation of the transcription initiation complex on mammalian rdna.
title_unstemmed Formation of the transcription initiation complex on mammalian rDNA.
topic Cell Biology, Molecular Biology
url http://dx.doi.org/10.1128/mcb.6.10.3418