Slc11a1跨膜肽段的嵌膜结构和取向
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摘要
溶质转运蛋白1(Slc11a1)由12个预测跨膜区构成,它是二价金属离子传输体,具有重要的生物功能。哺乳动物的Slc11a1能够抵抗鼠伤寒沙门氏菌、分枝杆菌、杜氏利什曼原虫等病原微生物的感染。Slc11a1第四跨膜区的G169D突变会导致蛋白功能的丧失。Slc11同源体的电生理学研究发现第三跨膜区中一些保守性残基的突变会导致Slc11传输功能的降低或丧失。本论文中我们利用圆二色谱、荧光光谱和差示扫描量热方法研究了Slc11a1第二跨膜区(TM2)、第三跨膜区(TM3和E139A突变体)、第四跨膜区(TM4和G169D突变体)肽片段在模拟膜环境中的结构、取向及肽与膜的相互作用等,同时研究了残基突变带来的影响。结果表明这些跨膜肽段均插入模型膜的内部,与TM2和TM4相比,TM3在膜中的位置相对较浅并且受pH的影响较大。TM2和TM4在所有的膜模拟环境中均形成较好的α-螺旋结构,而TM3在含有阴离子头基的模型膜中形成α-螺旋结构。E139A突变增加了跨膜肽段的α-螺旋结构,同时消除了肽段在膜中取向的pH敏感性。G169D突变对跨膜肽段的拓扑结构影响不大,只影响肽段中色氨酸残基微环境极性的pH依赖性。TM2和TM4在膜中具有类似的拓扑结构。
Solute carrier family 11 member 1 is an integral membrane protein which plays an important role in the biological functions. It belongs to Slc11 family which is highly conserved from bacteria to human and is one of a few genes that demonstrated the parasitic resistance at the molecular level. Mammalian Slc11a1 is involved in defense against intracellular pathogens such as Salmonella typhimurium, Mycobacterium bovis and Leishmania donovan. For human, NRAMP1 is associated with the diseases such as tuberculosis, leprosy and rheumatoid arthritis, etc. Understanding the functional mechanism of Slc11a1 may be helpful to study the pathogenesis for these diseases. As a proton-coupled divalent metal ion transporter, Slc11a1 can transport essential metal ions for life including Fe~(2+) and Mn~(2+). People have a certain understanding for biological function of Slc11a1, but are still not clear for its functional mechanism. Some of the transmembrane segments of Slc11a1 may be closely related to the transfer activity of the protein, so the study of the peptides that are crucial for the function of the transporter is helpful to understand the structure and function of the integral protein.
Recently, it has become a widely used method in the structural studies of membrane proteins to select function-relating peptides from protein as model peptides and characterize them in the membrane-mimetic environments. The study on the model peptides corresponding to isolated transmembrane domains have been proved to be very useful in providing qualitative information for integral proteins. Both disease-causing mutations in Slc11a1 occurring at glycine 169 (G169D) and Slc11a2 occurring at glycine 185 (G185R) locate within TM4. It has been found by some electrophysiological studies of Slc11 homolog that the replacement of the conservative residues in TM3 severely affected or abrogated the transport function. TM2 is an extremely hydrophobic transmembrane segment and close to TM3. These means that each of the three transmembrane segments may play a specific role in the proton-coupled divalent metal ion transport of the homolog. Therefore, in this thesis, we studied the membrane-inserted structures and orientation of the peptides, including TM2, TM3/TM3-E139A and TM4/TM4-G169D of Slc11a1 in various membrane-mimetic environments, such as SDS micelles, DMPC and DMPG vesicles, using CD spectroscopy, DSC and Fluorescence spectroscopy.
First, the second structures of the peptides in model membranes and various pH values were studied using CD. The TM2 and TM4 related peptides adopt predominantlyα-helical conformations in all membrane-mimetic environments used in the study, while TM3 related peptides displayα-helical conformations in DMPG-containing vesicles and SDS micelles but basically are unstructured in DMPC. At all pH values (especially at pH 5.5 and 7) and membrane environments, TM3 is basically less structured than TM2 and TM4. The secondary structures of TM3 in various membranes show evident pH-dependence. The pH sensitivity of TM3 folding is associated to the protonation/deprotonation process of the residue Glu139. The deprotonation of Glu139 is unfavorable for theα-helical folding of TM3. The E139A substitution of TM3 increases theα-helix content and decreases the pH dependence of the helical folding. In comparison with TM3, TM2 and TM4 displays less pH sensitivity of the helical folding. The G169D mutation of TM4 enhances the pH sensitivity of the secondary structure. Moreover, TM4 may be self-associated in the model membranes containing anionic headgroups and more helicity of TM2 in the lipid mixtures at pH 5.5 could be explained for the self-association of the peptide.
Secondly, we studied the influences of the peptides on the phase transition behaviors of the model membranes using DSC measurement. We analyzed the peptide/membrane interactions through the changes in the calorimetric parameters of the phase transition of the model membranes in the presence and absence of the peptides. The DSC results showed that TM2, TM3 and TM4 are embedded in the lipid membranes. In pure DMPG and DMPC lipid bilayers, TM4 has more extensive perturbation to the hydrophobic chains of the lipid membranes and is embedded in the lipid bilayers more deeply than TM3. Moreover, the interactions of TM4 with membranes are less affected by pH, whereas the abnormality was observed at pH 5.5. The results studied in DMPG/DMPC lipid mixture also showed that TM3 has less extensive perturbation to the hydrocarbon chains of the lipids than both TM2 and TM4. The phase transition behaviors of the lipid mixture incorporated with peptides are more similar to those of DMPC lipid bilayers in the presence of peptides. The DSC result that the perturbation of TM2 to DMPG/DMPC mixture is less extensive at pH 5.5 than at pH 4 and 7 supports the suggestion that TM2 is self-associated in the mixed membrane at pH 5.5.
Finally, we used the quenching constants (Ksv) and the wavelengths of the maximum Trp emission (λmax) obtained by fluorescence measurements to analyze the orientation and location of the peptides in model membranes further. The results showed that TM2 and TM4 have similar topology in membranes and they are inserted more deeply than TM3, especially at pH 5.5 and 7. In addition, the locations of the two peptides are nearly not affected by pH. In contrast, the position of TM3 in membranes is adjusted by pH, more deeply at acidic solution, but less deeply at alkalescent solution. The pH dependence of TM3 is attributed to the protonation/deprotonation of Glu139 residue in the peptide. The pH sensitivity of the topological structure of TM3 in membranes was changed by the E139A substitution, implying that Glu139 plays an important role in the topological structure of TM3. The topological structure of TM4 is hardly affected by the G169D mutation which only increases the pH sensitivity of the Trp microenvironment.
We found in the study that the property of lipid headgroups strongly influences the secondary structure, interaction between peptide and membrane and orientation of the peptides. The transmembrane peptides have more helicity in SDS micelles and DMPG-containing vesicles than in zwitterionic DMPC vesicles, implying that the anionic lipid headgroups are favorable to induce anα-helical conformation. The helical stabilization of the TM peptides incorporated with anionic lipid vesicles or SDS micelles could be attributed to the electrostatic interactions between positively charged flanking residues at the N-termini of the peptides and anionic headgroups of lipids. TM3 is embedded in DMPC vesicles less deeply than in DMPG-containing lipid membranes. The stability of the DMPG/DMPC (1:2) mixed vesicles is more similar to that of DMPC vesicles in the presence of peptide, whereas the packing of the mixed vesicles is more similar to that of DMPG vesicles.
Solute carrier family 11 member 1 is an integral membrane protein which plays an important role in the biological functions. It belongs to Slc11 family which is highly conserved from bacteria to human and is one of a few genes that demonstrated the parasitic resistance at the molecular level. Mammalian Slc11a1 is involved in defense against intracellular pathogens such as Salmonella typhimurium, Mycobacterium bovis and Leishmania donovan. For human, NRAMP1 is associated with the diseases such as tuberculosis, leprosy and rheumatoid arthritis, etc. Understanding the functional mechanism of Slc11a1 may be helpful to study the pathogenesis for these diseases. As a proton-coupled divalent metal ion transporter, Slc11a1 can transport essential metal ions for life including Fe~(2+) and Mn~(2+). People have a certain understanding for biological function of Slc11a1, but are still not clear for its functional mechanism. Some of the transmembrane segments of Slc11a1 may be closely related to the transfer activity of the protein, so the study of the peptides that are crucial for the function of the transporter is helpful to understand the structure and function of the integral protein.
Recently, it has become a widely used method in the structural studies of membrane proteins to select function-relating peptides from protein as model peptides and characterize them in the membrane-mimetic environments. The study on the model peptides corresponding to isolated transmembrane domains have been proved to be very useful in providing qualitative information for integral proteins. Both disease-causing mutations in Slc11a1 occurring at glycine 169 (G169D) and Slc11a2 occurring at glycine 185 (G185R) locate within TM4. It has been found by some electrophysiological studies of Slc11 homolog that the replacement of the conservative residues in TM3 severely affected or abrogated the transport function. TM2 is an extremely hydrophobic transmembrane segment and close to TM3. These means that each of the three transmembrane segments may play a specific role in the proton-coupled divalent metal ion transport of the homolog. Therefore, in this thesis, we studied the membrane-inserted structures and orientation of the peptides, including TM2, TM3/TM3-E139A and TM4/TM4-G169D of Slc11a1 in various membrane-mimetic environments, such as SDS micelles, DMPC and DMPG vesicles, using CD spectroscopy, DSC and Fluorescence spectroscopy.
First, the second structures of the peptides in model membranes and various pH values were studied using CD. The TM2 and TM4 related peptides adopt predominantlyα-helical conformations in all membrane-mimetic environments used in the study, while TM3 related peptides displayα-helical conformations in DMPG-containing vesicles and SDS micelles but basically are unstructured in DMPC. At all pH values (especially at pH 5.5 and 7) and membrane environments, TM3 is basically less structured than TM2 and TM4. The secondary structures of TM3 in various membranes show evident pH-dependence. The pH sensitivity of TM3 folding is associated to the protonation/deprotonation process of the residue Glu139. The deprotonation of Glu139 is unfavorable for theα-helical folding of TM3. The E139A substitution of TM3 increases theα-helix content and decreases the pH dependence of the helical folding. In comparison with TM3, TM2 and TM4 displays less pH sensitivity of the helical folding. The G169D mutation of TM4 enhances the pH sensitivity of the secondary structure. Moreover, TM4 may be self-associated in the model membranes containing anionic headgroups and more helicity of TM2 in the lipid mixtures at pH 5.5 could be explained for the self-association of the peptide.
Secondly, we studied the influences of the peptides on the phase transition behaviors of the model membranes using DSC measurement. We analyzed the peptide/membrane interactions through the changes in the calorimetric parameters of the phase transition of the model membranes in the presence and absence of the peptides. The DSC results showed that TM2, TM3 and TM4 are embedded in the lipid membranes. In pure DMPG and DMPC lipid bilayers, TM4 has more extensive perturbation to the hydrophobic chains of the lipid membranes and is embedded in the lipid bilayers more deeply than TM3. Moreover, the interactions of TM4 with membranes are less affected by pH, whereas the abnormality was observed at pH 5.5. The results studied in DMPG/DMPC lipid mixture also showed that TM3 has less extensive perturbation to the hydrocarbon chains of the lipids than both TM2 and TM4. The phase transition behaviors of the lipid mixture incorporated with peptides are more similar to those of DMPC lipid bilayers in the presence of peptides. The DSC result that the perturbation of TM2 to DMPG/DMPC mixture is less extensive at pH 5.5 than at pH 4 and 7 supports the suggestion that TM2 is self-associated in the mixed membrane at pH 5.5.
Finally, we used the quenching constants (Ksv) and the wavelengths of the maximum Trp emission (λmax) obtained by fluorescence measurements to analyze the orientation and location of the peptides in model membranes further. The results showed that TM2 and TM4 have similar topology in membranes and they are inserted more deeply than TM3, especially at pH 5.5 and 7. In addition, the locations of the two peptides are nearly not affected by pH. In contrast, the position of TM3 in membranes is adjusted by pH, more deeply at acidic solution, but less deeply at alkalescent solution. The pH dependence of TM3 is attributed to the protonation/deprotonation of Glu139 residue in the peptide. The pH sensitivity of the topological structure of TM3 in membranes was changed by the E139A substitution, implying that Glu139 plays an important role in the topological structure of TM3. The topological structure of TM4 is hardly affected by the G169D mutation which only increases the pH sensitivity of the Trp microenvironment.
We found in the study that the property of lipid headgroups strongly influences the secondary structure, interaction between peptide and membrane and orientation of the peptides. The transmembrane peptides have more helicity in SDS micelles and DMPG-containing vesicles than in zwitterionic DMPC vesicles, implying that the anionic lipid headgroups are favorable to induce anα-helical conformation. The helical stabilization of the TM peptides incorporated with anionic lipid vesicles or SDS micelles could be attributed to the electrostatic interactions between positively charged flanking residues at the N-termini of the peptides and anionic headgroups of lipids. TM3 is embedded in DMPC vesicles less deeply than in DMPG-containing lipid membranes. The stability of the DMPG/DMPC (1:2) mixed vesicles is more similar to that of DMPC vesicles in the presence of peptide, whereas the packing of the mixed vesicles is more similar to that of DMPG vesicles.
引文
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