隋森芳
从事生物大分子复杂体系及生物膜的结构和功能的研究
个性化签名
- 姓名:隋森芳
- 目前身份:
- 担任导师情况:
- 学位:
-
学术头衔:
博士生导师
- 职称:-
-
学科领域:
生物化学
- 研究兴趣:从事生物大分子复杂体系及生物膜的结构和功能的研究
隋森芳1970年在清华大学毕业后留校任教。1980年在清华大学获理学硕士(固体物理)。1983年转入生物学研究领域。1988年在德国慕尼黑工业技术大学获自然科学博士学位(生物物理)。1989年至今任清华大学生物科学与技术系副教授、教授(1991-)、博士生导师,系主任(1992.12-1995.12)。隋森芳教授长期从事生物大分子复杂体系及生物膜的结构和功能的研究。他在PNAS(2003)上发表了大肠杆菌蛋白转运体SecA蛋白在膜上的环行结构,提出膜诱导SecA由水溶性蛋白转变为具有转运蛋白性质的内在膜蛋白的假说。他在PNAS(2003)上发表了突触囊泡syt蛋白在膜上的寡聚结构,提出syt 的寡聚化促进囊泡与突触前膜融合的模型。他在JBC(2002)上发表了诱发老年痴呆症的Ab蛋白的插膜可抑制其纤维化的新观点。隋森芳在2000年获中国高校科学技术奖(自然科学奖)一等奖。2001年获全国优秀博士论文博士生导师。2003年出版著作《膜分子生物学》。目前为国际重要学术杂志《Journal of Structural Biology》编委;《生物物理学报》副主编。
-
主页访问
2344
-
关注数
0
-
成果阅读
450
-
成果数
11
【期刊论文】Visualization of synaptotagmin I oligomers assembled onto lipid monolayers
隋森芳, Yi Wu*†, Yuhong He*†, Jihong Bai‡, Shang-Rong Ji*, Ward C. Tucker‡, Edwin R. Chapman‡§, and Sen-Fang Sui*§
PNAS February 18, 2003, Vol. 100, no.4, 2082-2087,-0001,():
-1年11月30日
Neuronal exocytosis is mediated by Ca21-triggered rearrangementsbetween proteins and lipids that result in the opening anddilation of fusion pores. Synaptotagmin I (syt I) is a Ca21-sensingprotein proposed to regulate fusion pore dynamics via Ca21-promoted binding of its cytoplasmic domain (C2A-C2B) to effectormolecules, including anionic phospholipids and other copies of syt.Functional studies indicate that Ca21-triggered oligomerization ofsyt is a critical step in excitation–secretion coupling; however, thisactivity has recently been called into question. Here, we show thatCa21 does not drive the oligomerization of C2A-C2B in solution.However, analysis of Ca21zC2A-C2B bound to lipid monolayers,using electron microscopy, revealed the formation of ring-likeheptameric oligomers that are '11 nm long and '11 nm indiameter. In some cases, C2A-C2B also assembled into long filaments.Oligomerization, but not membrane binding, was disruptedby neutralization of two lysine residues (K326,327) within the C2Bdomain of syt. These data indicate that Ca21 first drives C2AC2Bzmembraneinteractions, resulting in conformational changesthat trigger a subsequent C2B-mediated oligomerization step.Ca21-mediated rearrangements between syt subunits may regulatethe opening or dilation kinetics of fusion pores or may play arole in endocytosis after fusion.
-
48浏览
-
0点赞
-
0收藏
-
0分享
-
157下载
-
0评论
-
引用
【期刊论文】Ring-like pore structures of SecA: Implication for bacterial protein-conducting channels
隋森芳, Hong-Wei Wang*†, Yong Chen*†, Hsiuchin Yang‡, Xianchuan Chen‡, Ming-Xing Duan*, Phang C. Tai‡§, and Sen-Fang Sui*§
PNAS April 1, 2003, Vol. 100, no.7, 4221-4226,-0001,():
-1年11月30日
SecA, an essential component of the general protein secretion pathwayof bacteria, is present in Escherichia coli as soluble andmembrane-integral forms. Hereweshow by electron microscopy thatSecA assumes two characteristic forms in the presence of phospholipidmonolayers: dumbbell-shaped elongated structures and ring-likepore structures. The ring-like pore structures with diameters of 8 nmand holes of 2nm are found only in the presence of anionic phospholipids.These ring-like pore structures with larger 3- to 6-nm holes(without staining) were also observed by atomic force microscopicexamination. They do not form in solution or in the presence ofuncharged phosphatidylcholine. These ring-like phospholipidinducedpore-structures may form the core of bacterial proteinconductingchannels through bacterial membranes.
-
23浏览
-
0点赞
-
0收藏
-
0分享
-
94下载
-
0评论
-
引用
隋森芳, Zhanfang Ma and Sen-Fang Sui*
Angew. Chem. Int. Ed. 2002, 41, No.12,-0001,():
-1年11月30日
-
46浏览
-
0点赞
-
0收藏
-
0分享
-
142下载
-
0评论
-
引用
【期刊论文】Human Apolipoprotein H May Have Various Orientations When Attached to Lipid Layer
隋森芳, Fu Wang, Xiao-Feng Xia, and Sen-fang Sui
Biophysical Journal Volume 83 August 2002 985-993,-0001,():
-1年11月30日
Apolipoprotein H (ApoH), also known as β2-glycoprotein I, is a plasma glycoprotein with its in vivo physiological and pathogenic roles being closely related to its interaction with negatively charged membranes. Although the threedimensional crystal structure of ApoH has been recently solved, direct evidence about the spatial state of ApoH on the membrane is still lacking. In this work, the interactions of ApoH with the lipid layer are studied by a combination of lipid monolayer approach and surface concentration determination. The spatial state of the orientation of ApoH on the lipid layer is investigated by analyzing the process of membrane-attached ApoH molecules being extruded out from the phospholipid monolayer by compression. The results show that on neutral lipid layer ApoH has an upright orientation, which is not sensitive to the phase state of the lipid layer. However, on acidic lipid layer, ApoH may have two forms of orientation. One is an upright orientation in the liquid phase region, and the other is flat orientation on the condensed domain region. The variation of the spatial state of ApoH on the lipid layer may relate to a variety of its physiological functions.
-
52浏览
-
0点赞
-
0收藏
-
0分享
-
97下载
-
0评论
-
引用
隋森芳, Shang-Rong Ji, Yi Wu, and Sen-fang Sui‡
Vol. 277, No.8, Issue of February 22, pp. 6273-6279, 2002,-0001,():
-1年11月30日
β-Amyloid peptide (Aβ), a normal constituent of neuronal and non-neuronal cells, has been proven to be the major component of extracellular plaque of Alzheimer's disease. Interactions between Aβand neuronal membranes have been postulated to play an important role in the neuropathology of Alzheimer’s disease. Here we show that Aβ is able to insert into lipid bilayer. The membrane insertion ability of Aβ is critically controlled by the ratio of cholesterol to phospholipids. In a low concentration of cholesterol Aβ prefers to stay in membrane surface region mainly in aβ-sheet structure. In contrast, as the ratio of cholesterol to phospholipids rises above 30mol%, Aβ can insert spontaneously into lipid bilayer by its C terminus. During membrane insertion Aβ generates about 60%β-helix and removes almost all β-sheet structure. Fibril formation experiments show that such membrane insertion can reduce fibril formation. Our findings reveal a possible pathway by which Aβ prevents itself from aggregation and fibril formation by membrane insertion.
-
68浏览
-
0点赞
-
0收藏
-
0分享
-
203下载
-
0评论
-
引用
【期刊论文】The membrane insertion of trichosanthin is membrane-surface-pH dependent
隋森芳, Xiao-feng XIA and Sen-fang SUI
Biochem. J. (2000) 349, 835-841 (Printed in Great Britain),-0001,():
-1年11月30日
Trichosanthin (TCS) is the active component extracted from Tianhuafen, a traditional herbal medicine that has been used for abortion in China for centuries. It belongs to the type-I ribosomeinactivating protein (RIP) family and can inactivate the eukaryotic ribosome through its RNA N-glycosidase activity. Recentstudies have shown TCS to be multifunctional, its pharmacologicalproperties including immunomodulatory, anti-tumourand anti-HIV activities. The membrane-insertion property ofTCS is thought to be essential for its physiological effect, for itmust get across the membrane before it can enter the cytoplasmand exert its RIP function. In this paper, the membrane-insertionmechanism of TCS was studied. The monolayer experimentrevealed that TCS's membrane-insertion ability was dependenton low pH. Fluorescence spectroscopy using 1-anilinonaph-thalene-8-sulphonic acid as a probe showed that low pH mayinduce the conformational change of TCS that leads to thehydrophobic-site exposure, and the CD result showed that thisconformational change did not alter its secondary structure.Such conformational change leads to an intermediate state,called the molten globular state' by previous investigators. ThepH-dependent membrane insertion and conformational changewere related by the fact that the optimal membrane-surface pHneeded was the same for the two events. From these and otherresults, a membrane-insertion model was proposed.
conformational change,, lipid-protein interaction,, membrane surface pressure,, molten globular state,, ribosomeinactivatingprotein.,
-
40浏览
-
0点赞
-
0收藏
-
0分享
-
99下载
-
0评论
-
引用
【期刊论文】Membrane-induced conformational change in human apolipoprotein H
隋森芳, Shao-Xiong WANG, Yu-Tong SUN and Sen-Fang SUI
Biochem. J. (2000) 348, 103-106 (Printed in Great Britain),-0001,():
-1年11月30日
The interaction of apolipoprotein H (Apo H) with lipid membrane has been considered to be a basic mechanism for the biological function of the protein. Previous reports have demonstratedthat Apo H can interact only with membranes containinganionic phospholipids. Here we study the membrane-inducedconformational change of Apo H by CD spectroscopy with twodifferent model systems: anionic-phospholipid-containing liposomes[such as 1,2-dimyristoyl-sn-glycero-3-phosphoglycerol(DMPG) and cardiolipin], and the water}methanol mixtures atmoderately low pH, which mimic the micro-physicochemicalenvironment near the membrane surface. It is found that Apo Hundergoes a remarkable conformational change on interactionwith liposomes containing anionic phospholipid. To interact withliposomes containing DMPG, there is a 6.8%increase in a-helixin the secondary structures; in liposomes containing cardiolipin,however, there is a 12.6% increase in a-helix and a 9% decreasein b-sheet. The similar conformation change in Apo H can beinduced by treatment with an appropriate mixture of water}methanol. The results indicate that the association of Apo Hwith membrane is correlated with a certain conformationalchange in the secondary structure of the protein.
circular dichroism,, β2-glycoprotein I,, lipid-proteininteraction,, protein adsorption., related to its biological function,,
-
42浏览
-
0点赞
-
0收藏
-
0分享
-
65下载
-
0评论
-
引用
-
32浏览
-
0点赞
-
0收藏
-
0分享
-
54下载
-
0评论
-
引用
【期刊论文】Membrane-induced conformational change of proteins
隋森芳, Sen-fang Sui
Advances in Colloid and Interface Science 85(2000)257-267,-0001,():
-1年11月30日
Many proteins exhibit both a water-soluble and a membrane-bound state. The proteins in the membrane-bound state obtain a distinct structure from that in the bulk, which exists in many important biological processes. In the present paper we would stress that the variation of the physical chemistry properties of the microenvironment adjacent to the membranesurface region play an important role in the process of the membrane-induced conformational changes of the proteins.
Lipid protein interaction, Protein conformation, Membrane insertion, Protein adsorption
-
29浏览
-
0点赞
-
0收藏
-
0分享
-
72下载
-
0评论
-
引用
隋森芳, Shao-Xiong Wang, Guo-ping Cai, and Sen-fang Sui*
Biochemistry 1999, 38, 9477-9484,-0001,():
-1年11月30日
Apolipoprotein H (ApoH) is a plasma glycoprotein with its in vivo physiological and pathogenic roles being closely related to its interaction with negatively charged membranes. In this paper, the interaction of ApoH with phospholipid vesicles was characterized by (i) detecting the wavelength shift of the fluorescence spectrum of ApoH and (ii) measuring the fluorescence quenching extent of ApoH by the membrane resident quencher 1-palmitoyl-2-stearoyl-(5-doxyl)-sn-glycero-3-phosphocholine (DPC). The observed blue shift upon addition of DMPG vesicles indicated that the tryptophan residues of ApoH moved from a polar to a nonpolar environment. The insertion ability of ApoH into PG-containing v esicles did not depend on the PG content in a stoichiometric way as did the blue shift, indicating that the negatively charged DMPG does not serve as a specific binding site but rather provides a suitable microenvironment for ApoH interaction. The finding that the detachment effect of cations on the blue shift is remarkably different from that on the quenching extent suggests that ApoH is capable of existing in two different conformations when membrane-bound.
-
38浏览
-
0点赞
-
0收藏
-
0分享
-
87下载
-
0评论
-
引用