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Accumulation of the β-subunit of polygalacturonase 1 in normal and mutant tomato fruit (1993)

Pogson, Barry J. ; Brady, Colin J.

Springer

Planta 191 (1993), S. 71-78

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ISSN: 1432-2048

Keywords: Fruit ripening ; Lycopersicon (fruit ripening) ; Mutant (tomato) ; Polygalacturonase (β-subunit)

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract Polyclonal antiserum raised against the native PG1 isoform of tomato fruit (Lycopersicon esculentum Mill.) polygalacturonase [poly(1,4-α-d-galacturonide) glycanohydrolase, EC 3.2.1.15] bound to each of the subunits of the protein and also to a range of other fruit proteins. Affinity purification was used to remove antibody molecules that bound to the native form of the PG2 isoform. The resulting serum bound to native PG1, denatured PG2 and β-subunits of PG1 but not to native PG2 or other fruit proteins. This anti-PG1 serum was used to monitor the occurrence of the PG1 β-subunit and PG2 in detergent extracts of tomato tissues. The β-subunit polypeptide was detected in pericarp but not locule tissue of fruit, including fruit of the rin and nor mutants. It increased in amount in the pericarp tissues from an early stage to the mature green stage, clearly prior to any appreciable accumulation of the PG2 subunit. The β-subunit polypeptide was not detected in stem or leaf tissues. A PG2-specific antiserum was used to study the interaction of PG2 with the isolated β-subunit. The PG2 isoform was bound to the β-subunit over a wide range of salt concentrations and pH; the interaction was independent of the presence of reducing agents. It is concluded that strong non-covalent forces are involved in the interaction. The results are consistent with a model in which the β-subunit is positioned in the cell wall structure and provides a specific binding site for the active PG2 subunit when this is synthesised during ripening.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00240897

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Identification of a program of contractile protein gene expression initiated upon skeletal muscle differentiation (1993)

Sutherland, Colin J. ; Esser, Karyn A. ; Elsom, Vicki L. ; [et al.]

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

Developmental Dynamics 196 (1993), S. 25-36

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ISSN: 1058-8388

Keywords: Contractile protein genes ; Skeletal muscle ; Regeneration ; Differentiation ; Rodent ; Human ; Genetic program ; Life and Medical Sciences ; Cell & Developmental Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Medicine

Notes: The functional diversity of skeletal muscle is largely determined by the combinations of contractile protein isoforms that are expressed in different fibers. Just how the developmental expression of this large array of genes is regulated to give functional phenotypes is thus of great interest. In the present study, we perform a comprehensive analysis of contractile protein isoform mRNA profiles in skeletal muscle systems representing each generation of fiber formed: primary, secondary, and regenerating fibers. We find that in each system examined there is a common pattern of isoform gene expression during early differentiation for 5 of the 6 gene families we have investigated: myosin light chain (MLC)1, MLC2, tropomyosin, troponin (Tn)C, and TnI. We suggest that the common isoform patterns observed together represent a genetic program of skeletal muscle differentiation that is independent of the mature fiber phenotype and is found in all newly formed myotubes. Within each of these contractile protein gene families the program is independent of the isoforms of myosin heavy chain (MHC) expressed. The maintenance of such a program may reflect a specific requirement of the initial differentiation process. © 1993 wiley-Liss, Inc.

Additional Material: 4 Ill.