Evidence for polyphosphate in phosphorylated nonhistone nuclear proteins

Offenbacher, Steven; Kline, Edward S.

doi:10.1016/0003-9861(84)90368-0

Cited by 33 publications

(14 citation statements)

References 40 publications

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“…The removal of phosphate groups from NSP5 could have also contributed to this change of apparent molecular mass, as they are sensitive to alkaline hydrolysis (Juhl & Soderling, 1983;Offenbacher & Kline, 1984). We now confirmed (Fig.…”

Section: Discussionsupporting

confidence: 76%

Phosphorylation Generates Different Forms of Rotavirus NSP5

Afrikanova

Miozzo

Giambiagi

et al. 1996

Journal of General Virology

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Section: Discussionsupporting

confidence: 76%

Phosphorylation Generates Different Forms of Rotavirus NSP5

Afrikanova

Miozzo

Giambiagi

et al. 1996

Journal of General Virology

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“…The concentration of polyphosphates is controlled by enzymes involved in their synthesis and degradation such as polyphosphate kinase (EC 2.7.4.1); polyphosphate‐glucose phosphotransferase (EC 2.7.1.63); 3‐phosphoglyceroyl‐phosphate‐polyphosphate phosphotransferase (EC 2.7.4.17); endopolyphosphatase (EC 3.6.1.10) and exopolyphosphatase (EC 3.6.1.11) [4–6,8]. Polyphosphates have been implicated in several cellular processes and in the control of the level of ATP and pyrophosphate, both the center of two very important metabolic crossroads [5,6,13,14].…”

Section: Discussionmentioning

confidence: 99%

Polyphosphates strongly inhibit the tRNA dependent synthesis of poly(A) catalyzed by poly(A) polymerase from Saccharomyces cerevisiae

Sillero¹,

Diego²,

Silles³

et al. 2003

FEBS Letters

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Polyphosphates of di¡erent chain lengths (P 3 , P 4 , P 15 , P 35 ), (1 W WM) inhibited 10, 60, 90 and 100%, respectively, the primer (tRNA) dependent synthesis of poly(A) catalyzed poly(A) polymerase from Saccharomyces cerevisiae. The relative inhibition evoked by p 4 A and P 4 (1 W WM) was 40 and 60%, respectively, whereas 1 W WM Ap 4 A was not inhibitory. P 4 and P 15 were assayed as inhibitors of the enzyme in the presence of (a) saturating tRNA and variable concentrations of ATP and (b) saturating ATP and variable concentrations of tRNA. In (a), P 4 and P 15 behaved as competitive inhibitors, with K i values of 0.5 W WM and 0.2 W WM, respectively. In addition, P 4 (at 1 W WM) and P 15 (at 0.3 W WM) changed the Hill coe⁄cient (n H ) from 1 (control) to about 1.3 and 1.6, respectively. In (b), the inhibition by P 4 and P 15 decreased V and modi¢ed only slightly the K m values of the enzyme towards tRNA. ß

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“…Poly P is a polyanion with some resemblance to nucleic acids, and interacts with basic proteins and the basic domains of proteins such as non-histone nuclear proteins (Offenbacher & Kline 1984;reviewed in Kornberg 1995). As expected from its acidic nature, poly P inhibits transcription by both Ej 70 and Ej 38 holoenzyme at a potassium glutamate concentration of 50 mM (see Fig.…”

Section: Discussionmentioning

confidence: 99%