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Molecular and Cellular Biology, July 2000, p. 4959-4969, Vol. 20, No. 14
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

The 2'-5' Oligoadenylate/RNase L/RNase L Inhibitor Pathway Regulates Both MyoD mRNA Stability and Muscle Cell Differentiation

C. Bisbal,1,* M. Silhol,1 H. Laubenthal,1 T. Kaluza,1 G. Carnac,2 L. Milligan,1 F. Le Roy,1 and T. Salehzada1,dagger

EP 2030 and UMR 5535 CNRS, 34293 Montpellier Cedex 5,1 and IGH CNRS UPR 1142, 34396 Montpellier Cedex 5,2 France

Received 28 December 1999/Returned for modification 16 February 2000/Accepted 6 April 2000

The 2'-5' oligoadenylate (2-5A)/RNase L pathway is one of the enzymatic pathways induced by interferon. RNase L is a latent endoribonuclease which is activated by 2-5A and inhibited by a specific protein known as RLI (RNase L inhibitor). This system has an important role in regulating viral infection. Additionally, variations in RNase L activity have been observed during cell growth and differentiation but the significance of the 2-5A/RNase L/RLI pathway in these latter processes is not known. To determine the roles of RNase L and RLI in muscle differentiation, C2 mouse myoblasts were transfected with sense and antisense RLI cDNA constructs. Importantly, the overexpression of RLI in C2 cells was associated with diminished RNase L activity, an increased level of MyoD mRNA, and accelerated kinetics of muscle differentiation. Inversely, transfection of the RLI antisense construct was associated with increased RNase L activity, a diminished level of MyoD mRNA, and delayed differentiation. In agreement with these data, MyoD mRNA levels were also decreased in C2 cells transfected with an inducible RNase L construct. The effect of RNase L activity on MyoD mRNA levels was relatively specific because expression of several other mRNAs was not altered in C2 transfectants. Therefore, RNase L is directly involved in myoblast differentiation, probably through its role in regulating MyoD stability. This is the first identification of a potential mRNA target for RNase L.

* Corresponding author. Mailing address: IGH CNRS UPR 1142, 141 route de la Cardonille, 34396 Montpellier Cedex 5, France. Phone: 33-4-67-61-36-58. Fax: 33-4-67-04-02-45. E-mail: bisbal{at}jones.igm.cnrs-mop.fr.

dagger Present address: IGH CNRS UPR 1142, 34396 Montpellier Cedex 5, France.

Molecular and Cellular Biology, July 2000, p. 4959-4969, Vol. 20, No. 14
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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