Cellular and subcellular distribution of saporins, type-1 ribosome-inactivating proteins, in soapwort (Saponaria officinalis L.)

Planta ◽  
1994 ◽  
Vol 194 (4) ◽  
pp. 461-470 ◽  
Author(s):  
Raffaella Carzaniga ◽  
Lesley Sinclair ◽  
Anthony P. Fordham-Skelton ◽  
Nick Harris ◽  
Ronald R. D. Croy
Planta ◽  
2008 ◽  
Vol 228 (6) ◽  
pp. 963-975 ◽  
Author(s):  
Augusto Parente ◽  
Barbara Conforto ◽  
Antimo Di Maro ◽  
Angela Chambery ◽  
Paolo De Luca ◽  
...  

2020 ◽  
pp. 193-212
Author(s):  
Marco R. Soria ◽  
Luca Benatti ◽  
Gianpaolo Nitti ◽  
Aldo Ceriotti ◽  
Michela Solinas ◽  
...  

1996 ◽  
Vol 319 (2) ◽  
pp. 507-513 ◽  
Author(s):  
Luigi BARBIERI ◽  
Paola VALBONESI ◽  
Paola GORINI ◽  
Annalisa PESSION ◽  
Fiorenzo STIRPE

The ribosome-inactivating proteins (RIPs) are a family of plant enzymes for which a unique activity has been determined: rRNA N-glycosidase, which removes adenine at a specific universally conserved position (A4324 in the case of rat ribosomes). Here we report that saporin-L1, a RIP from the leaves of Saponaria officinalis, recognizes other substrates, including RNAs from different sources, DNA and poly(A). Saporin-L1 depurinated DNA extensively and released adenine from all adenine-containing polynucleotides tested. Adenine was the only base released from DNA or artificial polynucleotides. The characteristics of the reactions catalysed by saporin-L1 have been determined: optimal pH and temperature, ionic requirements, and the kinetic parameters Km and kcat. The reaction proceeded without cofactors, at low ionic strength, in the absence of Mg2+ and K+. Saporin-L1 had no activity towards various adenine-containing non-polynucleotide compounds (cytokinins, cofactors, nucleotides). This plant protein may now be classified as a polynucleotide:adenosine glycosidase.


2020 ◽  
pp. 128337
Author(s):  
Nicola Landi ◽  
Maria Rosaria Ruocco ◽  
Sara Ragucci ◽  
Federica Aliotta ◽  
Rosarita Nasso ◽  
...  

2006 ◽  
Vol 80 (13) ◽  
pp. 6657-6668 ◽  
Author(s):  
Michael L. Gatza ◽  
Susan J. Marriott

ABSTRACT Human T-cell leukemia virus type 1 Tax is a predominantly nuclear viral oncoprotein that colocalizes with cellular proteins in nuclear foci known as Tax speckled structures (TSS). Tax is also diffusely distributed throughout the cytoplasm, where it interacts with and affects the functions of cytoplasmic cellular proteins. Mechanisms that regulate the distribution of Tax between the cytoplasm and nucleus remain to be identified. Since Tax has been shown to promote genome instability by perturbing cell cycle progression and DNA repair mechanisms following DNA damage, we examined the effect of genotoxic stress on the subcellular distribution and interacting partners of Tax. Tax localization was altered in response to various forms of cellular stress, resulting in an increase in cytoplasmic Tax and a decrease in Tax speckled structures. Concomitantly, colocalization of Tax with sc35 (a TSS protein) decreased following stress. Tax translocation required the CRM1 nuclear export pathway, and a transient interaction between Tax and CRM1 was observed following stress. These results suggest that the subcellular distribution of Tax and the interactions between Tax and cellular proteins respond dynamically to cellular stress. Changes in Tax distribution and interacting partners are likely to affect cellular processes that regulate cellular transformation.


1994 ◽  
Vol 58 (8) ◽  
pp. 1458-1462 ◽  
Author(s):  
José Miguel Ferreras ◽  
Carlos Alegre ◽  
Rosario Iglesias ◽  
Tomás Girbes

FEBS Letters ◽  
1998 ◽  
Vol 428 (1-2) ◽  
pp. 75-79 ◽  
Author(s):  
Fernando M de Benito ◽  
Rosario Iglesias ◽  
José Miguel Ferreras ◽  
Lucı́a Citores ◽  
Emilio Camafeita ◽  
...  

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