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Journal of Virology, March 2006, p. 2495-2505, Vol. 80, No. 5
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.5.2495-2505.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

A Novel Alternative Splicing Isoform of Human T-Cell Leukemia Virus Type 1 bZIP Factor (HBZ-SI) Targets Distinct Subnuclear Localization

Ken Murata,1* Toshihisa Hayashibara,1,{dagger} Kazuyuki Sugahara,1 Akiko Uemura,1 Taku Yamaguchi,2 Hitomi Harasawa,1 Hiroo Hasegawa,1 Kazuto Tsuruda,1 Toshiro Okazaki,1 Takehiko Koji,3 Takayuki Miyanishi,2 Yasuaki Yamada,1 and Shimeru Kamihira1*

Department of Laboratory Medicine, Nagasaki University Graduate School of Biomedical Sciences, Sakamoto 1-7-1, Nagasaki 852-8501, Japan,1 Faculty of Environmental Studies, Nagasaki University, Bunkyo 1-14, Nagasaki 852-8521, Japan,2 Department of Histology and Cell Biology, Nagasaki University Graduate School of Biomedical Sciences, Sakamoto 1-12-4, Nagasaki 852-8501, Japan3

Received 19 July 2005/ Accepted 2 December 2005

Adult T-cell leukemia (ATL) is associated with prior infection with human T-cell leukemia virus type 1 (HTLV-1); however, the mechanism by which HTLV-1 causes adult T-cell leukemia has not been fully elucidated. Recently, a functional basic leucine zipper (bZIP) protein coded in the minus strand of HTLV-1 genome (HBZ) was identified. We report here a novel isoform of the HTLV-1 bZIP factor (HBZ), HBZ-SI, identified by means of reverse transcription-PCR (RT-PCR) in conjunction with 5' and 3' rapid amplification of cDNA ends (RACE). HBZ-SI is a 206-amino-acid-long protein and is generated by alternative splicing between part of the HBZ gene and a novel exon located in the 3' long terminal repeat of the HTLV-1 genome. Consequently, these isoforms share >95% amino acid sequence identity, and differ only at their N termini, indicating that HBZ-SI is also a functional protein. Duplex RT-PCR and real-time quantitative RT-PCR analyses showed that the mRNAs of these isoforms were expressed at equivalent levels in all ATL cell samples examined. Nonetheless, we found by Western blotting that the HBZ-SI protein was preferentially expressed in some ATL cell lines examined. A key finding was obtained from the subcellular localization analyses of these isoforms. Despite their high sequence similarity, each isoform was targeted to distinguishable subnuclear structures. These data show the presence of a novel isoform of HBZ in ATL cells, and in addition, shed new light on the possibility that each isoform may play a unique role in distinct regions in the cell nucleus.

* Corresponding author. Present address for Ken Murata: Faculty of Medicine, Division of Hematology/Clinical Laboratory Medicine, Tottori University, Nishi-machi 36-1, Yonago, Tottori 683-8504, Japan. Phone: 81-859-34-8537. Fax: 81-859-34-8132. E-mail: kmurata{at}grape.med.tottori-u.ac.jp. Mailing address for Shimeru Kamihira: Department of Laboratory Medicine, Nagasaki University Graduate School of Biomedical Sciences, Sakamoto 1-7-1, Nagasaki 852-8501, Japan. Phone: 81-95-849-7407. Fax: 81-95-849-7422. E-mail: kamihira{at}net.nagasaki-u.ac.jp.

{dagger} Present address: Department of Internal Medicine, Ureshino Onsen Hospital, Shimozyuku 1919, Ureshino, Fujitsu, Saga 843-0301, Japan.

Journal of Virology, March 2006, p. 2495-2505, Vol. 80, No. 5
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.5.2495-2505.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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