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The VirD2 protein of Agrobacterlum tumefaciens carries nuclear localization signals important for transfer of T-DNA to plants (1993)

Rossi, L. ; Hohn, B. ; Tinland, B.

Springer

Molecular genetics and genomics 239 (1993), S. 345-353

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ISSN: 1617-4623

Keywords: β-Glucuronidase ; Transient expression ; Ti plasmid ; Nuclear localization signal ; Tobacco seedling

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Agrobacterium tumefaciens is able to transfer a piece of DNA, the T-DNA, to the nucleus of the plant cell. The VirD2 protein is required for the production of the T-DNA, it is tightly linked to the T-DNA and it is thought to direct it to the plant genome. Two nuclear localization signals (NLS), one in the N-terminal part and one in the C-terminal part of the VirD2 protein, have been shown to be able to target marker proteins to the plant nucleus. Here we analyze nuclear entry of the T-DNA complex using a new and very sensitive assay for T-DNA transfer. We show that optimal T-DNA transfer requires the VirD2 NLS located in the C-terminal part of the protein, whereas mutations in the N-terminal NLS coding sequence seem to have no effect on T-DNA transfer.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00276932

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Red blood cell phagocytosis following hexokinase inactivation (1994)

Chiarantini, L. ; Antonelli, A. ; Rossi, L. ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Cell Biochemistry and Function 12 (1994), S. 217-220

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ISSN: 0263-6484

Keywords: Hexokinase ; red blood cells ; IgG-binding ; phagocytosis ; C3 ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Medicine

Notes: Hexokinase inactivating antibodies were loaded into human erythrocytes using an encapsulation procedure based on hypotonic haemolysis, isotonic resealing and reannealing. Red blood cells loaded with anti-hexokinase IgG showed 20 percent residual hexokinase activity and reduced glycolytic activity. 9Incubation of these cells in the presence of an oxidizing agent such as terbutyl hydroperoxide (TBH) and then in autologous plasma, promoted opsonization by autologous IgG and complement deposition, but not haemolysis. Furthermore, the antihexokinase IgG loaded cells treated with TBH were actively recognized and phagocytosed by macrophages. Thus, metabolic impairment of human erthrocytes promotes autologous IgG binding, C3 deposition and phagocytosis, a mechanism already reported for the removal of senescent erythrocytes.

Additional Material: 2 Ill.