Associate Professor of Genetics, Dipartimento di Genetica, Università di Napoli Federico II.

Research
The laboratory focuses on the mechanisms underlying transcription regulation during the mammalian cell cycle in normal and pathological conditions. Specifically, the role of dedicated cyclin-dependent kinases and phosphatases involved in the reversible phosphorylation status of the carboxyl-terminal domain (CTD) of the RNA polymerase II (RNAPII) has been investigated, with particular regard to the function of the cyclin-dependent kinase CDK9 and the CTD phosphatase FCP1 in the process of transcription elongation. In parallel, the group is using a proteomic approach to isolate FCP1 interacting proteins.
The laboratory aims to gain a better understanding of the regulatory mechanisms underlying the cyclic and reversible phosphorylation of RNA polymerase II (RNAPII) during cell proliferation and transformation. We are currently searching for the interaction proteins of the cyclinT/Cdk9 complex and FCP1 by using a proteomic approach.

Selected publications
Napolitano G, Mazzocco A, Fraldi A, Majello B, Lania L. Functional inactivation of Cdk9 through oligomerization chain reaction. Oncogene 2003;31:4882-8.

Licciardo P, Amente S, Ruggiero L, Monti M, Pucci P, Lania L, Majello B. The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP. Nucleic Acids Res 2003;3:999-1005.

Majello B, Napolitano G. Control of RNA polymerase II activity by dedicated CTD kinases and phosphatases. Front Biosci 2001;6:D1358-68 (Review).

Licciardo P, Ruggiero L, Lania L, Majello B. Transcription activation by targeted recruitment of the RNA polymerase II CTD phosphatase FCP1. Nucleic Acids Res 2001;17:3539-45.

Licciardo P, Napolitano G, Majello B, Lania,G. Inhibition of Tat transactivation by the RNA polymerase II CTD-phosphatase FCP1. AIDS 2001;15:301