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RNA-assisted nuclear transport of the meiotic regulator Mei2p in fission yeast

Article Abstract:

The dot formation exhibited in the meiotic prophase nuclei and induced by the Mei2p RNA-binding protein was analyzed to determine the role of the polyadenylated RNA molecule, meiRNA, in the nuclear localization of Mei2p. Mei2p acts with meiRNA in the promotion of meiosis I and cells lacking meiRNA fail to undergo the first meiotic division. It was discovered that meiRNA induced the Mei2p movement to the nucleus and colocalized with the Mei2p dot at the meiotic prophase. Mei2p accumulated in the cytoplasm when expressed alone but moved to the nucleolus when meiRNA was coexpressed.

Author: Yamashita, Akira, Yamamoto, Masayuki, Watanabe, Yoshinori, Nukina, Nobuyuki
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
Carrier proteins, Transport proteins, Cell nuclei, Cell nucleus

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Eliminating all obstacles: regulated proteolysis in the eukaryotic cell cycle

Article Abstract:

Two studies conducted by RMR Feldman et al and D. Skowyra et al have shown that the F-box protein Cdc-4 cannot bind to unphosphorylated Sic1 but can bind to phospho-Sic1. Interaction with the C-terminal WD-repeat domain of Cdc4 can generate binding. The discovery of several F-box-containing proteins indicates that specific protein kinase combinations may target proteins for degradation in diverse biological regulatory contexts. Findings reveal that Cdc20 and Hct1/Cdh1 can direct the anaphase-promoting complex to two distinct classes of mitotic substrates.

Author: Hoyt, M. Andrew
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
Eukaryotic cells, Cells (Biology), Eukaryotes, Proteolysis

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Molecular mimicry in development: identification of ste11+ as a substrate and mei3+ as a pseudosubstrate inhibitor of ran1+ kinase

Article Abstract:

The role of the ste11+ transcription factor and the mei3+ gene in ran+1 kinase inhibition is investigated. Ste11+ is shown to be a substrate for ran1+ in vitro, a reaction that is directly inhibited by mei3+, and is also revealed to have two domains homologous to each other and tp a domain of mei3+. Data point to sequences essential for the phosphorylation of ste11+ by ran1+ and indicate that mei3+ uses a pseudosubstrate mechanism to perform inhibition.

Author: Li, Peng, McLeod, Maureen
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
Mimicry (Biology)

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Subjects list: Research, Meiosis, Protein kinases
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