Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP).

Karttunen JT; Lehner PJ; Gupta SSHewitt EWCresswell P

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Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP).

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The ATP-binding cassette (ABC) transporter TAP translocates peptides from the cytosol to awaiting MHC class I molecules in the endoplasmic reticulum. TAP is made up of the TAP1 and TAP2 polypeptides, which each possess a nucleotide binding domain (NBD). However, the role of ATP in peptide binding and translocation is poorly understood. We present biochemical and functional evidence that the NBDs of TAP1 and TAP2 are non-equivalent. Photolabeling experiments with 8-azido-ATP demonstrate a cooperative interaction between the two NBDs that can be stimulated by peptide. The substitution of key lysine residues in the Walker A motifs of TAP1 and TAP2 suggests that TAP1-mediated ATP hydrolysis is not essential for peptide translocation but that TAP2-mediated ATP hydrolysis is critical, not only for translocation, but for peptide binding.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2001年第13期|7431-7436|共6页
作者
Karttunen JT; Lehner PJ; Gupta SSHewitt EWCresswell P;
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作者单位

Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, 310 Cedar Street, New Haven, CT 06510, USA.;

o.state.ct.us;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
ABC Transporters; Adenosine Triphosphate; Major Histocompatibility Complex; ABC转运子; 腺苷三磷酸; 主要组织相容性复合物;

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Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP).

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