Structure and Regulatory Properties of Eucaryotic RNA Polymerase

Blatti, S. P.; Ingles, C J; Lindell, Thomas J.; Morris, Paul W.; Weaver, Robert F.; Weinberg, Fanyela; Rutter, William J.

doi:10.1101/sqb.1970.035.01.080

Cited by 206 publications

(94 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Gels 4,5 and 6 correspond to gels 1, 2 and 3, respectively. The relation between enzymes BI and BII and RNA polymerase type II which was identified by Roeder and Rutter in rat liver [8] and also purified from calf thymus [9] is somewhat obscure. The fact that Blatti et al [9] found only the bands corresponding to subunits B2 and B3 in their calf thymus preparation suggests that enzyme BI was lost during the purification, and that their calf thymus enzyme II is mainly enzyme BII.…”

Section: Discussionmentioning

confidence: 98%

“…The relation between enzymes BI and BII and RNA polymerase type II which was identified by Roeder and Rutter in rat liver [8] and also purified from calf thymus [9] is somewhat obscure. The fact that Blatti et al [9] found only the bands corresponding to subunits B2 and B3 in their calf thymus preparation suggests that enzyme BI was lost during the purification, and that their calf thymus enzyme II is mainly enzyme BII. On the other hand, we have found (see the following paper) that RNA polymerase type II (as defined by Roeder and Rutter [8] ), when purified from rat liver, corresponds mainly to enzyme BI.…”

Section: Discussionmentioning

confidence: 98%

See 1 more Smart Citation

Structural evidence for two α‐amanitin sensitive RNA polymerases in calf thymus

1971

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 98%

Structural evidence for two α‐amanitin sensitive RNA polymerases in calf thymus

1971

View full text Add to dashboard Cite

“…Polymerase I is localized in the nucleolus (2); its RNA product has the base composition and hybridization behavior expected of ribosomal RNA (3). These data indicate that the major role of this enzyme is to synthesize ribosomal RNA, although it may transcribe a limited number of other RNA species.…”

mentioning

confidence: 95%

Molecular Structures of DNA-Dependent RNA Polymerases (II) from Calf Thymus and Rat Liver

Weaver

Blatti

Rutter

1971

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

107

View full text Add to dashboard Cite

DNA-dependent RNA polymerase II has been purified to high specific activity and apparent homogeneity from both calf thymus and rat liver. Two form II enzymes are present in rat-liver preparations, one with the molecular structure 1(190,000)i(150,000),(35,000)1(25,000)dl, the other with a molecular structureof [(170,000),(150,000) -(35,000),(25,000),] (molecular weights are within ±5% but the absolute values are approximate). Inclusion of a proteolytic inhibitor during the isolation procedure decreases the proportion of the molecule containing the 170,000 subunit. Calf-thymus RNA polymerase preparations typically exhibit four components on polyacrylamide gels that contain sodium dodecyl sulfate, with an apparent molecular structure of [(190,000)1(150,000),(35,000)1-(25,000)i]. In addition, some calf-thymus polymerase II preparations contain small quantities of the [(170,OO)1-(150,000)i(35,000)1(25,000)iJ species; the quantity of this species may also be increased from less than 5% in the normal preparation to at least 40% in an "aged" preparation. Thus, the 170,000 subunit may be derived from the 190,000 subunit in both tissues. Until unequivocal evidence is obtained on this point, however, the possibility that the large subunits are unique species should not be eliminated. The general structural similarity of the eukaryotic RNA polymerase II with that of the prokaryotic polymerase suggests that the modes of action and regulation may be analogous.Multiple forms of DNA-dependent RNA polymerases have been shown to exist in eukaryotic cells (1, 2). Polymerase I is localized in the nucleolus (2); its RNA product has the base composition and hybridization behavior expected of ribosomal RNA (3). These data indicate that the major role of this enzyme is to synthesize ribosomal RNA, although it may transcribe a limited number of other RNA species. Polymerase II, on the other hand, is found in the nucleoplasm (2). Its product has a more DNA-like base composition and is competed well in hybridization-competition experiments by whole nuclear RNA (3), suggesting that this polymerase synthesizes the bulk of the nucleoplasmic RNA species. A role for polymerase III, believed to be present in the nucleoplasm, has yet to be elucidated. The mushroom toxin, aamanitin, selectively inhibits polymerase II, while forms I and III are not affected (4,5

show abstract

“…It is tempting to speculate that the different polymerase species have differing transcription specificities. Forms A1 and B constitute the major proportion of the total RNA polymerase activity of the nucleus (the other forms making up less than It is already known that the form A1 polymerase is localised in the nucleolus [34] and, from work on Xenopus oocytes [38] and with rat-liver nuclei [39], it is apparent that the form A1 polymerase is responsible for the transcription of the ribosomal cistrons. This paper now demonstrates, that under specific conditions, transcription of interphase chromatin is carried out exclusively by the form B (a-amanitin sensitive) DNA-dependent RNA polymerase of rat liver.…”

mentioning

confidence: 99%

Transcription of Mammalian Chromatin by Mammalian DNA‐Dependent RNA Polymerases

Butterworth

Cox²,

Chesterton

1971

European Journal of Biochemistry

186

View full text Add to dashboard Cite

The transcription of rat-liver chromatin has been studied using partially purified form A1 and highly purified form B DNA-dependent RNA polymerases isolated from rat liver. Chromatin contains endogenous RNA polymerase activity. This activity is evident only when the RNA polymerase assays are carried out a t high ionic strength and its appearance as the ionic-strength increases is thought to be due to the removal of chromatin-associated proteins which block further transcription by the bound enzyme. This activity is insensitive to the rifampicin derivative AF/O-13 which is shown to inhibit initiation of RNA synthesis by mammalian RNA polymerases. Form A1 polymerase is virtually inactive in the transcription of chromatin whereas the form B RNA polymerase (ol-amanitin sensitive) actively transcribes chromatin. This activity has two salt concentration optima: (a) 0.01 M (NH,),SO, or 0.03 M KC1; (b) 0.16 M (NH,),SO, or 0.25 M KC1. Both these activities are inhibited by rifampicin AF/0-13. A comparison of the activity of the rat-liver form B polymerase and the Micrococcus lysodeikticus RNA polymerase demonstrates that chromatin is a more efficient template for the rat-liver enzyme. Evidence is presented that the rat-liver form B and the Micrococcus lysodeikticus RNA polymerases bind to and transcribe from Werent sites on the chromatin DNA.

show abstract

Structure and Regulatory Properties of Eucaryotic RNA Polymerase

Cited by 206 publications

References 0 publications

Structural evidence for two α‐amanitin sensitive RNA polymerases in calf thymus

Structural evidence for two α‐amanitin sensitive RNA polymerases in calf thymus

Molecular Structures of DNA-Dependent RNA Polymerases (II) from Calf Thymus and Rat Liver

Transcription of Mammalian Chromatin by Mammalian DNA‐Dependent RNA Polymerases

Contact Info

Product

Resources

About