Multiple, independently regulated, polyadenylated messages for histone H3 and H4 in<i>Tetrahymena</i>

Bannon, Gary A.; Calzone, Frank J.; Bowen, Josephine; Allis, C. David; Gorovsky, Martin A.

doi:10.1093/nar/11.12.3903

Cited by 79 publications

(56 citation statements)

References 31 publications

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“…Tetrahymena macronuclear DNA was isolated as described previously (9) except that proteinase K was used instead of Pronase. DNA was digested with restriction endonucleases according to standard procedures (48) or manufacturers' instructions.…”

Section: Methodsmentioning

confidence: 99%

Four distinct and unusual linker proteins in a mitotically dividing nucleus are derived from a 71-kilodalton polyprotein, lack p34cdc2 sites, and contain protein kinase A sites.

Wu¹,

Allis²,

Sweet³

et al. 1994

Mol. Cell. Biol.

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Section: Methodsmentioning

confidence: 99%

Four distinct and unusual linker proteins in a mitotically dividing nucleus are derived from a 71-kilodalton polyprotein, lack p34cdc2 sites, and contain protein kinase A sites.

Wu¹,

Allis²,

Sweet³

et al. 1994

Mol. Cell. Biol.

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“…1A), a much greater difference than that observed between the major and minor H3s of other organisms. The major H3 genes are expressed during vegetative growth and repressed during starvation, while the minor H3.3 gene is constitutively expressed in growing and starved cells (4). The major H3 localizes to both MACs and MICs, while the minor H3.3 was found only in MACs.…”

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confidence: 98%

Deposition and Function of Histone H3 Variants in Tetrahymena thermophila

Cui

Liu

Gorovsky

2006

Molecular and Cellular Biology

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In Tetrahymena, HHT1 and HHT2 genes encode the same major histone H3; HHT3 and HHT4 encode similar minor H3 variants (H3s), H3.3 and H3.4. Green fluorescent protein (GFP)-tagged H3 is deposited onto chromatin through a DNA replication-coupled (RC) pathway. GFP-tagged H3.3 and H3.4 can be deposited both by a transcription-associated, replication-independent (RI) pathway and also weakly by an RC pathway. Although both types of H3s can be deposited by the RC pathway, DNA repair synthesis associated with meiotic recombination utilizes H3 specifically. The regions distinguishing H3 and H3.3 for their deposition pathways were identified. RC major H3 is not essential. Cells can grow without major H3 if the minor H3s are expressed at high levels. Surprisingly, cells lacking RI H3s are also viable and maintain normal nucleosome density at a highly transcribed region. The RC H3 is not detectably deposited by the RI pathway, even when there are no RI H3s available, indicating that transcription-associated RI H3 deposition is not essential for transcription. Minor H3s are also required to produce viable sexual progeny and play an unexpected role in the germ line micronuclei late in conjugation that is unrelated to transcription.

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“…Gels were fragmented into 0.5-cm pieces, and each chamber was loaded with five or six fragments. Elution was done for 2 In some cases, TBP antibodies were affinity purified essentially as described previously (52), with the following modifications. Bacterially expressed pET-TBP fusion protein was blotted to nitrocellulose (MSI).…”

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confidence: 99%

TATA-binding protein and nuclear differentiation in Tetrahymena thermophila.

Stargell¹,

Gorovsky²

1994

Mol. Cell. Biol.

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Unambiguous TATA boxes have not been identified in upstream sequences of Tetrahymena thermophila genes analyzed to date. To begin a characterization of the promoter requirements for RNA polymerase II, the gene encoding TATA-binding protein (TBP) was cloned from this species. The derived amino acid sequence for the conserved C-terminal domain of Tetrahymena TBP is one of the most divergent described and includes a unique 20-amino-acid C-terminal extension. Polyclonal antibodies generated against a fragment of Tetrahymena TBP recognize a 36-kDa protein in macronuclear preparations and also cross-react with yeast and human TBPs.Immunocytochemistry was used to examine the nuclear localization of TBP during growth, starvation, and conjugation (the sexual phase of the life cycle). The transcriptionaily active macronuclei stained at all stages of the life cycle. The transcriptionally inert micronuclei did not stain during growth or starvation but surprisingly stained with anti-TBP throughout early stages of conjugation. Anti-TBP staining disappeared from developing micronuclei late in conjugation, corresponding to the onset of transcription in developing macronuclei. Since micronuclei do not enlarge or divide at this time, loss of TBP appears to be an active process. Thus, the transcriptional differences between macro-and micronuclei that arise during conjugation are associated with the loss of a major component of the basal transcription apparatus from developing micronuclei rather than its appearance in developing macronuclei.TATA-binding protein (TBP) is required for transcription by all three nuclear RNA polymerases. TBP, along with an assortment of distinct TBP-associated factors, has been found to make up the RNA polymerase I selectivity factor I (9, 36), the polymerase II general transcription factor IID (14,73,83), and the RNA polymerase III general transcription factor IIIB (38,43,62,72,75). Given the need for TBP to function in these different complexes in such fundamental cellular processes, it is not surprising that TBP is highly conserved throughout eukaryotes. Yeast and human TBP are functionally interchangeable in basal transcription reactions reconstituted with yeast or human components (5,17,39) and have nearly identical TATA element binding specificities (78). The C-terminal 180 residues of TBP from a variety of organisms are typically 80% identical in amino acid sequence, whereas the N-terminal regions are divergent both in length and in amino acid sequence (6, 16, 20, 26, 28-30, 33, 37, 49, 55, 61). The C-terminal domain is necessary and sufficient for TATA element binding and basal transcription in vitro (28,41,55) and for the essential functions of yeast TBP in yeast cells (10,21,57,84). This region forms an independent structural domain within the context of the intact protein (41). It contains an interrupted repeat of 67 amino acids, a short basic repeat, and a region weakly homologous with bacterial sigma factors (10, 80). In addition to its role in the basal transcription apparatus, TBP also ...

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Multiple, independently regulated, polyadenylated messages for histone H3 and H4 inTetrahymena

Cited by 79 publications

References 31 publications

Four distinct and unusual linker proteins in a mitotically dividing nucleus are derived from a 71-kilodalton polyprotein, lack p34cdc2 sites, and contain protein kinase A sites.

Four distinct and unusual linker proteins in a mitotically dividing nucleus are derived from a 71-kilodalton polyprotein, lack p34cdc2 sites, and contain protein kinase A sites.

Deposition and Function of Histone H3 Variants in Tetrahymena thermophila

TATA-binding protein and nuclear differentiation in Tetrahymena thermophila.

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