Novel BNIP1 variants and their interaction with BCL2 family members

By PCR and EST database searches we have identified three novel BNIP1 splice variants, and found that one of them, BNIP1-b, contains a highly conserved BH3 domain. The BNIP1 gene has been assigned to chromosome 5q33–34. Using in vitro protein-protein interaction assays, all BNIP1 variants were shown...

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Veröffentlicht in:	FEBS letters 1999-04, Vol.448 (1), p.23-27
Hauptverfasser:	Zhang, Hong, Heim, Jutta, Meyhack, Bernd
Format:	Artikel
Sprache:	eng
Schlagworte:	Alternative Splicing Amino Acid Sequence Base Sequence BAX bcl-2-Associated X Protein bcl-X Protein BCL2 BCL2A1, BCL2-related protein A1 (previously Bfl-1) BCL2L1 BCL2L1, BCL2-like 1 (previously Bcl-xL) BH3, BCL2 homology region 3 BNIP1 BNIP1, BCL2/adenovirus E1B 19 kDa interacting protein 1 (previously Nip1) BNIP1vs, BNIP1 splice variants, including BNIP1-a, BNIP1-b and BNIP1-c (previously: Nip1s1, Nip1s2 and Nip1s3) CAT, chloramphenicol acetyltransferase DNA, Complementary EST, expressed sequence tag GST, glutathione S-transferase Humans Interaction Molecular Sequence Data PAGE, polyacrylamide gel electrophoresis PCR, polymerase chain reaction Proteins - genetics Proteins - metabolism Proto-Oncogene Proteins - genetics Proto-Oncogene Proteins - metabolism Proto-Oncogene Proteins c-bcl-2 - genetics Proto-Oncogene Proteins c-bcl-2 - metabolism STS, sequence tagged site Variant
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Zusammenfassung:	By PCR and EST database searches we have identified three novel BNIP1 splice variants, and found that one of them, BNIP1-b, contains a highly conserved BH3 domain. The BNIP1 gene has been assigned to chromosome 5q33–34. Using in vitro protein-protein interaction assays, all BNIP1 variants were shown to interact with BCL2 and also with BCL2L1 (previously Bcl-xL). These interactions are BH3-independent. Furthermore, the BNIP1 variants cannot interact with BAX. The results suggest that the BNIP1 variants are novel members of the BCL2 family but function through a mechanism different from other BH3-only members.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(99)00335-X