Polyamine activation of staphylococcal nuclease

Frank, Joseph J.; Hawk, Inez A.; Levy, Carl C.

doi:10.1016/0005-2787(75)90014-3

Cited by 23 publications

(16 citation statements)

References 14 publications

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“…In the case of nuclease I from rye germ ribosomes, it was noted that low concentrations (0.1 mM) of polyamines such as putrescine and spermidine inhibited ribonuclease activity, whereas higher concentrations (2.5 mM) had a stimulatory e¡ect [100]. Similar observations were made with Staphylococcal nuclease [162]. Thus, at low concentrations, polyamines act by changing the electrostatic potential of the enzyme^substrate complex and participate in the regulation of nucleic acid levels in cells by controlling nuclease activity [163].…”

Section: Inducers Activators and Inhibitorssupporting

confidence: 68%

Single-strand-specific nucleases

Desai

2003

FEMS Microbiology Reviews

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Single-strand-specific nucleases are multifunctional enzymes and widespread in distribution. Their ability to act selectively on singlestranded nucleic acids and single-stranded regions in double-stranded nucleic acids has led to their extensive application as probes for the structural determination of nucleic acids. Intracellularly, they have been implicated in recombination, repair and replication, whereas extracellular enzymes have a role in nutrition. Although more than 30 single-strand-specific nucleases from various sources have been isolated till now, only a few enzymes (S1 nuclease from Aspergillus oryzae, P1 nuclease from Penicillium citrinum and nucleases from Alteromonas espejiana, Neurospora crassa, Ustilago maydis and mung bean) have been characterized to a significant extent. Recently, some of these enzymes have been cloned, their crystal structures solved and their interactions with different substrates have been established. The detection, purification, characteristics, structure^function correlations, biological role and applications of single-strand-specific nucleases are reviewed.

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Section: Inducers Activators and Inhibitorssupporting

confidence: 68%

Single-strand-specific nucleases

Desai

2003

FEMS Microbiology Reviews

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“…Moreover, a low concentration (0.1 mM) of polyamines such as putrescine and spermidine inhibited the RNase activity of rye germ ribosomal nuclease I [47]. On the contrary, the DNase and RNase activities of S. aureus nuclease were stimulated by low amounts of putrescine, spermine and spermidine, whereas at high concentrations they inhibited both the activities [113]. However, endonuclease from barley aleurone layers was not a¡ected by putrescine, spermidine and spermine at 1 mM [102].…”

Section: Activators and Inhibitorsmentioning

confidence: 80%

Sugar non-specific endonucleases

Rangarajan¹

2001

FEMS Microbiology Reviews

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Sugar non-specific endonucleases are multifunctional enzymes and are widespread in distribution. Apart from nutrition, they have also been implicated in cellular functions like replication, recombination and repair. Their ability to recognize different DNA structures has also been exploited for the determination of nucleic acid structure. Although more than 30 non-specific endonucleases have been isolated to date, very little information is available regarding their structure^function correlations except that of staphylococcal and Serratia nucleases. However, during the past few years, the primary structure, nature of the active site based on sequence homology, and the probable mechanism of action have been postulated for some of the enzymes. This review describes the purification, characteristics, biological role and applications of sugar non-specific endonucleases. ß

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“…4, lane 4) had the same deleterious effect on association of Oct-2 with the three cellular proteins as did addition of EtdBr (lane 2). The effect of micrococcal nuclease treatment was prevented by the addition of EGTA (lane 6), which inhibits micrococcal nuclease activity (34). Treatment of the immunoprecipitates with RNase had no effect on recovery of Oct-2 or the three associated proteins (lane 8) As a control to demonstrate that EtdBr does not generally affect protein association in this assay, we tested its effect on the association of a GST-EiA 13S fusion protein with in vitro-translated piO5Rb (15,16).…”

Section: Resultsmentioning

confidence: 99%

Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations.

Lai

Herr

1992

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

438

302

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DNA-dependent and DNA-independent associations of DNA-binding proteins are important in transcriptional regulation. The analysis of DNA-independent associations frequently relies on assaying protein interaction in the absence of target DNA sequences. We have found that contaminating DNA in protein preparations can stabilize DNAdependent associations that may appear DNA-independent. Three cellular proteins of 70, 85, and 110 kDa coimmunoprecipitated with the octamer motif-binding protein Oct-2 because of the presence of contaminating DNA in the cell extracts. In addition, heterodimer formation between Oct-i (or Oct-2) and Pit-i during protein-affinity chromatography was stabilized by the contaminating DNA. In both instances, these DNAdependent protein associations were selectively inhibited by ethidlum bromide in the precipitation reaction without any evident effect on DNA-independent protein associations. Thus, ethidlum bromide may serve as a simple and general indicator of DNA-dependent and DNA-independent protein associations.Transcriptional regulation depends not only on the interactions between sequence-specific DNA-binding proteins and their respective cis-regulatory elements but also on the interactions among these proteins and with other components of the transcriptional machinery (reviewed in refs. 1-3). The availability of tools for studying sequence-specific transcription factors (e.g., cDNA clones and antibodies) has allowed more detailed analysis of the mechanisms by which proteinprotein interactions, both DNA-dependent and DNAindependent, regulate transcription. Current methods for determining DNA-independent protein-protein interactions include coimmunoprecipitation and protein-affinity chromatography. We have used coimmunoprecipitation to identify proteins that associate with the octamer motif-binding proteins Oct-1 (OTF-1, NFIII) and Oct-2 (OTF-2). These transcription factors are particularly interesting because they display the same DNA-binding specificity (4) and share very similar DNA-binding POU domains (5, 6) but display qualitatively different RNA polymerase II transcriptional activation properties. Oct-1 is an effective activator of small nuclear RNA-type promoters, whereas Oct-2 is an effective activator of mRNA-type promoters (7). Therefore, it is likely that Oct-1 and Oct-2 interact preferentially with different components of the transcriptional machinery.We identified four cellular proteins of 68, 70, 85, and 110 kDa that coimmunoprecipitated with Oct-2 from labeled cell extracts in what appeared to be a DNA-independent manner. We noticed, however, that the 70-, 85-, and 110-kDa proteins could bind DNA on their own. We subsequently identified the 70-and 85-kDa proteins as the two heterologous subunits of the human autoantigen Ku, which possesses strong nonspecific DNA-binding properties (ref. 8 and references therein). This observation suggested that the association of these three proteins with Oct-2 might be mediated by contaminating DNA in the labeled cell extracts. Consisten...

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Polyamine activation of staphylococcal nuclease

Cited by 23 publications

References 14 publications

Single-strand-specific nucleases

Single-strand-specific nucleases

Sugar non-specific endonucleases

Ethidium bromide provides a simple tool for identifying genuine DNA-independent protein associations.

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