Germinal center-associated nuclear protein (GANP) has a phosphorylation-dependent DNA-primase activity that is up-regulated in germinal center regions

Kazuhiko Kuwahara, Shinjirou Tomiyasu, Satoru Fujimura, Kazumi Nomura, Yan Xing, Noriko Nishiyama, Michio Ogawa, Shinobu Imajoh-Ohmi, Shunji Izuta, Nobuo Sakaguchi

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Antigen stimulation induces a rapid proliferation of B cells for expansion of specific B cell clones and their further differentiation into antibody-producing cells in germinal centers of T-dependent antigen-immunized mice. Previously, we identified a 210-kDa germinal center-associated nuclear protein (GANP) that is up-regulated selectively in germinal centers and carries an MCM-binding domain in the carboxyl-terminal side. In addition, here, we found a region (from 414 to 550 aa) in GANP molecule that is slightly similar to the known DNA-primase component p49. The recombinant GANP fragment covering this region synthesizes RNA primers for extension by DNA polymerase I with single-stranded DNA templates in vitro. GANP DNA-primase activity is controlled by phosphorylation at Ser502 that is induced by CD40-mediated signaling in vitro and in the germinal center B cells stimulated with antigen in vivo. Overexpression of ganp cDNA in Daudi B cells caused the increased DNA synthesis more than the levels of the mock-transfectants. These evidences suggested that the novel DNA-primase GANP is involved in regulation of cell proliferation of antigen-driven B cells in germinal centers.

Original languageEnglish
Pages (from-to)10279-10283
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume98
Issue number18
DOIs
Publication statusPublished - 28-08-2001

All Science Journal Classification (ASJC) codes

  • General

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