Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae.

Qin, Shiliang; Xie, A.; Bonato, M. Christina M.; McLaughlin, Calvin S.

doi:10.1016/s0021-9258(19)39916-8

Cited by 78 publications

(11 citation statements)

References 75 publications

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“…The deduced amino acid sequence for the Candida gene exhibits a high degree of identity to that of the Saccharomyces gene. Conservation between the two EF-3 proteins in the region containing nucleotide-binding motifs and poly-lysine blocks (7) supports the idea that these features are involved in the ribosome-dependent ATPase activity.…”

Section: Introductionsupporting

confidence: 57%

“…The alignment of the two sequences is shown in Figure 5 along with features of a putative functional domain of EF-3. These features, which include nucleotide-binding motifs of a putative ATPase active site and poly-lysine blocks proposed to be involved in ribosome interaction (7), are conserved in the CEF-3 amino acid sequence. The only exception to the above being a single change of an alanine for a cysteine in region A of the first nucleotidebinding motif.…”

Section: Resultsmentioning

confidence: 99%

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Isolation and sequence analysis of the gene for translation elongation factor 3 fromCandida albicans

Myers

Fonzi

Sypherd³

1992

Nucl Acids Res

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Elongation factor 3 (EF-3) is a unique and essential component of the translational system in fungi. The gene, CEF-3, encoding elongation factor 3 has been isolated from the dimorphic fungus Candida albicans. A heterologous gene probe containing the coding region of the EF-3 gene from Saccharomyces cerevisiae (YEF-3) was used to screen three Candida albicans genomic DNA libraries. The nucleotide sequences of four partial clones were determined and combined for a full-length of 3,671 base pairs (bp). A continuous open reading frame (ORF) of 3,147 bp encoding a predicted protein of 1,049 amino acids and Mr of 116,739 daltons has been identified. A transcript of 3,400 nucleotides is seen in Northern blot hybridization of Candida albicans total RNA using a CEF-3 gene probe. The single locus CEF-3 gene maps to chromosome 5 in the genome. Comparison of the deduced amino acid sequences of CEF-3 and YEF-3 shows 77.6%. identity. A higher degree of identity, 86.5%, is found when comparing the carboxy-terminal portions of the two proteins. At the nucleotide level, comparison of the coding regions of the two genes exhibit 79% identity while the upstream and downstream regions show 46% and 40% identity, respectively.

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Section: Introductionsupporting

confidence: 57%

Section: Resultsmentioning

confidence: 99%

Isolation and sequence analysis of the gene for translation elongation factor 3 fromCandida albicans

Myers

Fonzi

Sypherd³

1992

Nucl Acids Res

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“…As shown in Fig. 2, these include the Drosophila segmentation gene product Armadillo and its vertebrate homologs, [3-catenin and plakoglobin (Riggleman et al, 1989;McCrea et al, 1991;Franke et al, 1989); the mammalian guanine nucleotide exchange factor smg-GDS (Kikuchi et al, 1992); regulatory subunits of protein phosphatase 2A from yeast and humans (van Zyl et al, 1992;Hemmings et al, 1990); the yeast translation elongation factor EF3 (Qin et al, 1990); and the conserved adaptor molecules from coated pits, et-and 13-adaptin (Kirchhausen et al, 1989;Robinson, 1989;Ponnambalan et al, 1990). All of these proteins contain 8-15 tandem repeats, consisting of ~42 amino acids each with amino acid residues at particular positions being conserved between the repeats and among the different proteins (Fig.…”

Section: Pendulin Is a Member Of A Superfamily Of Proteins With Armadillo (Arm) Repeatsmentioning

confidence: 99%

Pendulin, a Drosophila protein with cell cycle-dependent nuclear localization, is required for normal cell proliferation.

Küssel

Frasch

1995

The Journal of Cell Biology

116

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Abstract. We describe the dynamic intracellular localization of Drosophila Pendulin and its role in the control of cell proliferation. Pendulin is a new member of a superfamily of proteins which contains Armadillo (Arm) repeats and displays extensive sequence similarities with the Srpl protein from yeast, with RAG-1 interacting proteins from humans, and with the importin protein from Xenopus. Almost the entire polypeptide chain of Pendulin is composed of degenerate tandem repeats of ,'~42 amino acids each. A short NH2-terminal domain contains adjacent consensus sequences for nuclear localization and cdc2 kinase phosphorylation. The subcellular distribution of Pendulin is dependent on the phase of cell cycle. During interphase, Pendulin protein is exclusively found in the cytoplasm of embryonic cells. At the transition between G2 and M-phase, Pendulin rapidly translocates into the nuclei where it is distributed throughout the nucleoplasm and the areas around the chromosomes. In the larval CNS, Pendulin is predominantly expressed in the dividing neuroblasts, where it undergoes the same cell cycle-dependent redistribution as in embryos. Pendulin is encoded by the oho31 locus and is expressed both maternally and zygotically. We describe the phenotypes of recessive lethal mutations in the oho31 gene that result in a massive decrease or loss of zygotic Pendulin expression. Hematopoietic cells of mutant larvae overproliferate and form melanotic tumors, suggesting that Pendulin normally acts as a blood cell tumor suppressor. In contrast, growth and proliferation in imaginal tissues are reduced and irregular, resulting in abnormal development of imaginal discs and the CNS of the larvae. This phenotype shows that Pendulin is required for normal growth regulation. Based on the structure of the protein, we propose that Pendulin may serve as an adaptor molecule to form complexes with other proteins. The sequence similarity with importin indicates that Pendulin may play a role in the nuclear import of karyophilic proteins and some of these may be required for the normal transmission and function of proliferative signals in the cells.

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“…In step 3, one of the expected products of the exchange is a chromosome with an insertion of YIplac211 flanked by duplicated chromosomal sequences. A cell containing the reciprocal product containing the deletion (not shown) would probably not be viable, since YEF3 is an essential gene (32).…”

Section: Methodsmentioning

confidence: 99%

Transformation of Saccharomyces cerevisiae With Nonhomologous DNA: Illegitimate Integration of Transforming DNA into Yeast Chromosomes and in Vivo Ligation of Transforming DNA to Mitochondrial DNA Sequences

Schiestl

Dominska

Petes

1993

Molecular and Cellular Biology

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When the yeast Saccharomyces cerevisiae was transformed with DNA that shares no homology to the genome, three classes of transformants were obtained. In the most common class, the DNA was inserted as the result of a reaction that appears to require base pairing between the target sequence and the terminal few base pairs of the transforming DNA fragment. In the second class, no such homology was detected, and the transforming DNA was integrated next to a CTT or GTT in the target; it is likely that these integration events were mediated by topoisomerase I. The final class involved the in vivo ligation of transforming DNA with nucleus-localized linear fragments of mitochondrial DNA.

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Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae.

Cited by 78 publications

References 75 publications

Isolation and sequence analysis of the gene for translation elongation factor 3 fromCandida albicans

Isolation and sequence analysis of the gene for translation elongation factor 3 fromCandida albicans

Pendulin, a Drosophila protein with cell cycle-dependent nuclear localization, is required for normal cell proliferation.

Transformation of Saccharomyces cerevisiae With Nonhomologous DNA: Illegitimate Integration of Transforming DNA into Yeast Chromosomes and in Vivo Ligation of Transforming DNA to Mitochondrial DNA Sequences

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