為了總結(jié)2008年的科研工作，展示各研究組的科研成果，加強(qiáng)研究組間的學(xué)術(shù)交流與合作，促進(jìn)研究所整體科研水平的提高，我所將于2009年1月4 - 6日（地點(diǎn)另行通知）召開2008年度學(xué)術(shù)年會，會期3天?，F(xiàn)將有關(guān)事項通知如下：

 

        1．年會將安排大會特邀報告、研究組長學(xué)術(shù)報告、研究生學(xué)術(shù)報告、墻報交流等活動，同時將評選優(yōu)秀研究生學(xué)術(shù)報告和學(xué)術(shù)墻報。

 

        2．本次年會的學(xué)術(shù)報告（PI報告和研究生報告）由重點(diǎn)實驗室推薦產(chǎn)生，根據(jù)會期暫定PI報告8-10人；學(xué)生報告12-15人。

 

        3．每個研究組至少展出一份墻報。墻報按統(tǒng)一規(guī)格制作：110厘米（高）×80厘米（寬）。

 

        4．年會將編印學(xué)術(shù)報告摘要和墻報摘要，請報告人和研究組盡快撰寫有關(guān)摘要(“word”文本,英文撰寫，格式附后)，并于12月15日前將摘要傳至科研處吳雯英 (wywu@sibs.ac.cn)。

 

        5．每個研究組參加年會人數(shù)一般不超過5人（含PI和學(xué)生）。各研究組負(fù)責(zé)人、各中心平臺負(fù)責(zé)人、所聘顧問的會務(wù)費(fèi)由研究所承擔(dān)；其他人員的與會費(fèi)用(約650 元左右)由研究組承擔(dān)。

 

        6．請各研究組將本組參加年會的人員名單（標(biāo)明性別）于12月22日前告知辦公室秦正葳(zwqing@sibs.ac.cn)。

 

2008年11月18日

備注：

1. 大會特邀報告30分鐘，提問15分鐘；PI學(xué)術(shù)報告20分鐘，提問15分鐘；

   研究生報告10分鐘，提問10分鐘。

2．墻報請按統(tǒng)一規(guī)格制作：110公分（高）×80公分（寬）

 

 

Solution Structures of Ubiquitin-Binding Domains and their Binding Specificities with Ubiquitin

 

Aixin Song, Chenjie Zhou, Ziren Zhou, Jing Hong, Yonggang Chang,

Hongchang Gao, Donghai Lin, and Hongyu Hu

 

Ubiquitin (Ub) is a very important cellular signal that targets proteins for degradation or regulates their functions. Many proteins or domains are involved in this particular post-translational modification system. To understand the binding specificities of these small domains with Ub, which are vital to selection and regulation for diverse cellular processes, we determined several Ub-binding domains (UBD) derived from diverse Ub-related proteins, and investigated their binding specificities with Ub by NMR. These domains include ubiquitin-interacting motifs (UIM) from ataxin-3 (AT3-UIMs) and co-chaperone HSJ1a, and ubiquitin-associated domains (UBA) from BMSC-UbP (BMSC-UBA), E3 ligases c-Cbl (cUBA) and Cbl-b (UBAb).

The solution structure of AT3-UIMs includes two helices and a turn in the linker region. NMR titration revealed that both the motifs in the tandem UIMs can interact through the conserved residues with the Leu8-Ile44-Val70 hydrophobic patch of Ub. The single UIM1 and UIM2 of AT3 can also bind Ub, respectively, but with lower affinities. These results imply that interaction of the tandem UIMs with Ub may undergo with a cooperative manner between these two UIMs, suggesting that the cooperative interaction may have significant effect on the aggregation of polyglutamine tract in AT3 adjacent to the tandem UIMs.

All the three UBA domains having studied primarily consist of three a-helices with a hydrophobic patch. Chemical shift perturbation study revealed that the UBA domains bind with the conserved five-stranded b-sheet of Ub via hydrophobic interactions, except for cUBA that binds Ub very weakly. The hydrophobic surface distributions on the first helix play crucial roles in their differential affinities for Ub binding. The structural model of the BMSC-UBA domain complexed with Ub was constructed by chemical shift mapping combined with the program HADDOCK and confirmed by mutagenesis. This complex structure may provide structural insights into the interaction between UBA domains of Ub-associated proteins and Ub-like domains.