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0޽h ? ̙33  @L(     0@O9S"uu u`  9 Vñv[~ހXv\O(u    c 4A3o?n ̃\O(uMOp ,$D 0  6R90   %SReNAMTNAGKNvb 1 4|. _w~̃ˆ0 %[G̃ (WEDTAX[(W N Sñv\O(u0 %ñvYtTṽ~ހ^OX[(W1_ؚn0.1 ~0.2M |m-N0[ 2''#'&'&'& 'b(H  0޽h ? ̙33 NFP (      0 9S"uu up  9 ZR }[~̃~ހXv\O(u    6d9@`   PenicilliumNlv~T Ov1Y;m b6RNO+gzvN(lxNNehvޏc 4xOWN~̃~ހXv[te'`sSb6RZ|vTb Vdk PenicilliumN[ck(Wu@wv~̃ N;N/f[G+̃ gHe0ro }X  B =   S (A 3?Z|bg,$D 0H  0޽h ? ̙33Z  `((  (V (  0H9S"uu u0@  9 4Y6ZhT(zzperiplasmic space :$$$&  ( 049@j  * r ( 090  SyXzz0cMON~ހXN~ހKNvrz ipQl3'`~̃N4'`~̃GW g0Q-N+T gYyˆ}v( OYˆ}vv08hxvI{TyZv ЏgNir(ۏeQ~ހv~Tˆ}v NSS'`vSSOˆ}vI{0 &` 2^   `H ( 0޽h ? ̙338 p0x(  0@ 0 68P "Table 8. Representative periplasmic proteins in E. coli. Binding proteins For amino acids (e.g. histadine, arginine) For sugars (e.g. glucose, maltose) For vitamins (e.g. thiamine, vitamin B12) For ions (e.g. phosphate, sulfate) Biosynthetic enzymes For murein assembly (e.g. transglycosylases, carboxypeptidases, transpeptidases) For fimbrial subunit secretion and assembly (e.g. chaperonins) Degradative enzymes phosphatases proteases Detoxifying enzymes Beta-lactamases (e.g. penicillinase) Aminoglycoside-phosphorylating enzymes~: 8`Z*")"P>  $& ? &   %   H 0 0޽h ? ̙33 |t4 (  4 4  0p8S"uu u@  8 XY7Z~ހX:_cW~̃  b 4 68@P<  Z`$Su(SOprotoplast a$tb_SOspheroplast b$LW~̃L-form6."g$ g$33H   4 0@8   ( 2 4 0Ȑ833P @ |&Su(SOvyrp 10e~ހX :NWtb_ 20[sXOeanS a y_ fñ 30 gk NЏR 40 NlṼSOagV:N1YS8TDMOp  E gf3 'ff&ff'ff&ff 'ff&ff'ff OH 4 0޽h ? ̙33x ( <(  <N <  08S"uu u  8 8YNZ~ހ(cytoplastic membrane .& &&   < c 6A3o?~̃~ހv~gaP ,$D 0 < 6t8@P F L1.i_~ހ/f'}4~ހXQOSV~ހ(vNB\go [ g9_'`vJSf0.'' ##  'z < 6T8P D d2. ‰[Ryel 1)(XRy (2) b'`gr (3)5u\b/g (4)ñvYt3022 # #   #   #   #  3H < 0޽h ? ̙33: Dz(  D D c ,A-o?~ހp` ,$D 0R D 68 0 @1972t^SingerTNicolsoncQv~ހm`vL]!jWZ!&$&&$& &$. ( D  08S"uu u@  8 4. ~ހv~gNSf[~b@& '    D B8O  \~ހm`vL]!jW &f3 R D 680 @ :N/f1utb_ˆ}vNx cgqN~cRe_gbvAmSOvL]_ AmRv{|SRP[B\gbNvޏ~SO ˆ}v(ad[\N7heĉR0WoAm(Wx{|vwm mS_-N0,J <2J'  JH D 0޽h ? ̙33( Hh(  Hf H c >Afluidmosaic: H 0\8p@& bFigure 10. Fluid mosaic model of a biological membrane. In aqueous environments membrane phospholipids arrange themselves in such a way that they spontaneously form a fluid bilayer. Membrane proteins, which may be structural or functional, may be permanently or transiently associated with one side or the other of the membrane, or even be permanently built into the bilayer, while other proteins span the bilayer and may form transport channels through the membrane. " 2`ZH 7H H 0޽h ? ̙33T P(  P\ P c 4Alipids H P 0޽h ? ̙33\  X(  XR X s *x?x  X s A ?file:///E:/e^eN9Y/CHAPTER%20%233%20BACTERIAL%20ARCHITECTURE.files/cytomemb.gifCell MembraneP0H X 0޽h ? ̙33  2*`(  ` ` s *8P  8 n5. ~ހvR, &$$  ` 08 Bra) c6R~ހQYir(%{Qir(TN"^ir vЏ0Nbc b) ~c~ހQck8^nSvnO\\O(u c) Tb~ހXTy~RLPS0Z|0xXx TZir(I{'YRP[v:W@b d) ۏL'lSxxSbIQTxxSvNW0W e)SNϑN" (W~̃-N 5uP[ OTATPTbvGWMON~ހ f) cOkv@wupv^cOkЏR@bϑ0  2   H ` 0޽h ? ̙33 hB(  h  h 6O8 Table 6. Functions of the procaryotic plasma membrane. 1. Osmotic or permeability barrier 2. Location of transport systems for specific solutes (nutrients and ions) 3. Energy generating functions, involving respiratory and photosynthetic electron transport systems, establishment of proton motive force, and transmembranous, ATP-synthesizing ATPase 4. Synthesis of membrane lipids (including lipopolysaccharide in Gram-negative cells) 5. Synthesis of murein (cell wall peptidoglycan) 6. Assembly and secretion of extracytoplasmic proteins 7. Coordination of DNA replication and segregation with septum formation and cell division 8. Chemotaxis (both motility per se and sensing functions) 9. Location of specialized enzyme system8 6`Z"JU06Z:( +*  j XH h 0޽h ? ̙33   lL(  l l  09S"uu u   9 `Y NZQ|~$&   l S $A 3?SOP p,$D 0 l B9 , SO(mesosome).&, && l 69 a  V ~ހQ6b_bvNy{r0B\rb2Nrir N,MON~ހRˆvMObDя0,," ,p l 69 W r SOvR (1)SNb_b 2 N8hRˆ gsQ 3 {|f6e) (WR N[W,g N+T{| EeYNYt N(WX NnQ Vdk~vf+}Nxv YTirNbrbr;Yu(WvQ~ހXQOvQHTs+}r0SKN ipQl4'`~̃VvQX0Z|+TϑNOTNT^~gce EeGYNTZ|QT[ Nf6e) R N[v{|+Tϑؚ @bNS_YNbS{|nT (W~ހX N1\OQs'Yv ُ7h ~vf+}Nxv YTir1\gfnQ~ހX Vdk ǏYN1rT ~ހSHTer ُeQ~lĞI{~rge YgesSHTs~r0 $TR TH  0޽h ? ̙330  @(  ^ S    9 c $E @  9 6&&&Z|/f~ހX;NbN Q4xOWZ|~g0bb6RvQTbvir(O~ހX_c$O u@g{k~̃0   ñv0R }0 ñv(lysozyme):SReNAMvG1TNAGvC4KNb 1 4v|. 4xOWZ|/eg _w~̃ˆ0@bNSyYNpހX(v0 [G̃ (WEDTAX[(W N Sñv\O(u0 ñvYtTṽ~ހ^OX[(W1_ؚn0.1 ~0.2M |m-N0 @ O'-#"#"#"#" # ' -B.*H  0޽h ? ̙33&0 0$v(  $^ $S      $c $,  @   l 6 R }[~̃~ހXv\O(up N TNñv Vdk[~̃~ހvq_TN N=\v T0 Penicillin: the story of an antibiotic The antibacterial effect of penicillin was discovered by Alexander Fleming in 1929. He noted that a fungal colony had grown as a contaminant on an agar plate streaked with the bacterium Staphylococcus aureus, and that the bacterial colonies around the fungus were transparent, because their cells were lysing. Fleming had devoted much of his career to finding methods for treating wound infections, and immediately recognised the importance of a fungal metabolite that might be used to control bacteria. The substance was named penicillin, because the fungal contaminant was identified as Penicillium notatum. Fleming found that it was effective against many Gram positive bacteria in laboratory conditions, and he even used locally applied, crude preparations of this substance, from culture filtrates, to control eye infections. However, he could not purify this compound because of its instability, and it was not until the period of the Second World War (1939-1945) that two other British scientists, Florey and Chain, working in the USA, managed to produce the antibiotic on an industrial scale for widespread use. All three scientists shared the Nobel Prize for this work, and rightly so - penicillin rapidly became the "wonder drug" which saved literally millions of lives. It is still a "front line" antibiotic, in common use for some bacterial infections although the development of penicillin-resistance in several pathogenic bacteria now limits its effectiveness (see later). |%& ~ p &L%^j H $ 0޽h ? ̙33:0 @,(  ,^ ,S     ,c $  @   RD. hT(zzperiplasmic space SyXzz0cMON~ހXN~ހKNvrz ipQl3'`~̃N4'`~̃GW g0Q-N+T gYyˆ}v( OYˆ}vv08hxvI{TyZv ЏgNir(ۏeQ~ހv~Tˆ}v NSS'`vSSOˆ}vI{0 {^opGr027.028 ~̃~ހX5u\gqGr {^opGr026 G+~̃NG-4'`~̃~ހXk `    Z | H , 0޽h ? ̙33 0 Z R P8 (  8^ 8S    L  8c $ @    & Z|/f~ހXv;NbN Q4xOWZ|~gbb6RvQTbvir(Õ~ހX:_c0 &&'YYpe~̃~ހX:_cTT V NS̃SOQ萄vؚnS ˆ{kN0 && (uñvYtnNI{nnm-NvG+̃ SN_0R~ހXQNNSN[hQ1S [nSOeavSu(SO ! ! (uñvYtG-̃e_{ gTBR  YNNVYNxvX[(W NS0RdSR~ހX &^ gRkYu~ހXṽ~ހy:Ntb_SO0 &&&L-form~̃/f(WgNsXagN N@bb_bvS_W N][b6q`Q NGWSNu :ON[te ZW痄v~ހX N~c~̃vV gb_` HTsYb_` 1uN/fgHQVLister;Sf[xvzbSs Ee T0   'YYpe~̃~ހX:_cT V NS̃SOQ萄vؚnS ˆ{kN FO(WdkؚnagN N gv~̃VS_ NX[;m sSS:NL-form~̃0 &&&&,W~̃(W;Sf[ Nv͑'`  gN,W~̃N gN[vuR !!!Ǒ(uؚnW{QW\O,W~̃vNW{Q0 -------N_f9hnc̃~ހX:_cv z^ \ipQl3'`̃@bb_bv[hQ NKmQ~ހṽ~ހyprotoplast; \ipQl4'`̃@bb_bv0NOYuRXṽ~ހytb_SOspheroplast; Su(SOvyrp 1)e~ހX :NWtb_ 2)[sXOeanS a y_ fñ 3) gk NЏR 4) NlṼSOagV:Nl g8TDMOp 5)uirf[yr'`Oe tb_SOvyrp dwQSu(SOyrpY a)S gN[b'` SW{Q b)S͑eTb~ހX ,W~̃% 0SzSb_bv~ހX:w(RbhQ),wQYb_'`0SNuA~k,(WW{QW Nb_blNqˆ̃=0 gNS͑eTb~ހX0 *  u%ff*%f.  f  f]  f(%f f7#f[f " $$ (%(( ((%(( ( (%(( ((%(( ((%( (!(( ( (!(( ( (!((#((!(9(%(,,,, ,,f,,j,8IHj  l WH 8 0޽h ? ̙33:0 `@(  @^ @S     @c $q @   4. Cytoplasmic Membrane Made of a phospholipid bilayer with integral and peripheral proteins embedded. It maintains the selective permeability of the cell, has respiratory enzymes and during cell division the chromosome is linked to the cell membrane at a site called Mesosome. ~ހcell membrane Sy~ހ(cytoplasmic membrane b(plasmic membrane /f'}4(W~ހXQOvNB\1uxTˆ}v(~bvgo0[ g9_'`vJS'`0Ǐ(XRy0 b'`gr0Su(SO4xˆb5uP[>f_\‰[I{el SNf~ހvX[(W0 ~ހv~g(W5uP[>f_\ N‰[ ~ހHTf>fvSB\~g  (W N N$N*NfrB\9Y@wNEmrv-NB\0{^opGr032.033.034 :y~ހTxv~g The CYTOPLASMIC MEMBRANE is the structure that makes the cell possible as it is a SELECTIVE BARRIER that separates the highly organized machinery of a cell from the frightful chaos on the exterior. The cytoplasmic membrane is composed of a #PHOSPHOLIPID BILAYER in which are embedded the various proteins that control what goes in and out of a cell (Views of membranes and another view that can be manipulated and still another view that takes a lot of memory but shows much detail). The cytoplasmic membrane is fluid (like a soap bubble) and usually very DELICATE and easily ruptured if the supporting cell wall is removed. The inner portion of the cytoplasmic membrane is composed of lipid or fat molecules that make it impermeable to molecules that dissolve in water, but water itself can MOVE FREELY through the cytoplasmic membrane. This inner region is said to be #HYDROPHOBIC or "water hating". Because the cytoplasmic membrane is a bilayer, the lipid molecules face each other, placing the phosphate groups on the outer edges of the cytoplasmic membrane. Phosphate is #HYDROPHILIC and likes to associate with water molecules. Many of the proteins embedded in the lipid bilayer are TRANSPORT proteins that BIND specific molecules and carry them into or out of the cell as required. The proteins allow the cell to live in very dilute nutrient solutions because they soak up the nutrients like a selective "sponge" and bring in the rare nutrient molecules. Click here to look at some lipid molecules, chose the "gif" forms. 6N P1  : B :      Y # 8   ,   ^  X 9!0!0Ug!0lx!0!0^i!0,8!0H @ 0޽h ? ̙33x 0 80pL(  L^ LS    * Lc $  @   Bacterial membranes are composed of 40 percent phospholipid and 60 percent protein. The phospholipids are amphoteric molecules with a polar hydrophilic glycerol "head" attached via an ester bond to two nonpolar hydrophobic fatty acid tails, which naturally form a bilayer in aqueous environments. Dispersed within the bilayer are various structural and enzymatic proteins which carry out most membrane functions. At one time, it was thought that the proteins were neatly organized along the inner and outer faces of the membrane and that this accounted for the double track appearance of the membrane in electron micrographs. However, it is now known that while some membrane proteins are located and function on one side or another of the membrane, most proteins are partly inserted into the membrane, or possibly even traverse the membrane as channels from the outside to the inside. It is possible that proteins can move laterally along a surface of the membrane, but it is thermodynamically unlikely that proteins can be rotated within a membrane, which discounts early theories of how transport systems might work. The arrangement of proteins and lipids to form a membrane is called the fluid mosaic model, which is illustrated in Figure 10. 8$.  U 5.H L 0޽h ? ̙33  0 W O T (  T^ TS    I  Tc $\F @   sFigure 11. Generalized structure of a membrane lipids. (top). A phospholipid in the membrane of the bacterium Escherichia coli. The R1 and R2 positions on glycerol are substituted with saturated or monounsaturated fatty acids, with ester linkages to the glyceride. The R3 position is substituted with phosphatidylethanolamine, the most common substituent in this position in Bacteria. (bottom). An Archaeal membrane lipid. In contrast to bacterial phospholipids, which are glycerol esters of fatty acids, the lipids in membranes of Archaea are diethers of glycerol and long-chain, branched, saturated hydrocarbons called isoprenoids, which are made up of repeating C5 subunits. One of the major isoprenoids is the C20 molecule phytanol. The R3 position of glycerol is not substituted. The structure of archaeal membrane lipids is thought to be an adaptation to extreme environments such as hot and acidic conditions where Archaea prevail in nature. The membranes of Bacteria are structurally similar to the cell membranes of eukaryotes, except that bacterial membranes consist of saturated or monounsaturated fatty acids (never polyunsaturated fatty acids) and do not normally contain sterols (Figure 11a). The membranes of Archaea form phospholipid bilayers functionally equivalent to bacterial membranes, but archaeal lipids are saturated, branched, repeating isoprenoid subunits that attach to glycerol via an ether linkage (Figure 11b), as opposed to the ester linkage found in glycerides of eukaryotic and bacterial membrane lipids. The structure of archaeal membranes is thought to be an adaptation to their survival in extreme environments. tn`Z`Z6`Z? ! % + )F D >  B o` 4 * m  0 XH T 0޽h ? ̙33 0 d\\(  \^ \S    V \c $? @   ~Figure 6. Cartoon of cytoplasmic membrane, showing its complex composition of protein, carbohydrates and lipids. The proteins "float" in the lipid "sea". Some proteins span the membrane, while others are attached to only one side or the other, or to other proteins embedded in the cytoplasmic membrane. Water can pass freely through the cytoplasmic membrane, but most other molecules can not. One important characteristic of the cytoplasmic membrane is that PROTONS (H+) are unable to cross the cytoplasmic membrane. Click here to learn about the lipid bilayer. Click here to see more pictures of membranes along with a good discussion. >~pZ  - Q 7    B!0 !02=H \ 0޽h ? ̙33 0 dF(  d^ dS     dc $T @   < H d 0޽h ? ̙330 NFp(  p^ pS    @ pc $k @   v ~̃ N+T~|SONS~SOKN{|v~ހhV FOYipQl3'`̃v~ހQQ^8O bbSb_bb__Y7hvQ|~ NcO:NgyR@bvf'Yby0 gNQ|~] gN蕄v Ty YSO0}rSO0TvSO0 SOmesosome 1u~ހQ6b_bvNy{r0B\rbVr~g N,MON~ހRˆMObvQя0vQR;N/fOۏ~ހvb_bv^NW Oir(v Y6RSvQvNRy gsQ0 NR~̃-NSO:Nf>f Bacillus subtilis0B. licheniformis0Streptococcus faecalis0Micrococcus luteus0V  13:ySO(WgrSO Y6RTRy-Nv\O(u <rUrS  H p 0޽h ? ̙33rt#1!'6s>C-HLRX#^edhiUlqw}ݖ" b Oh+'0Q `h  ȾɫԭecgcŲȾ2Microsoft PowerPointP@ @6ઠ!@ uy GPg  P('& &&#TNPPd 2OMi & TNPP &&TNPP     'A x(xʦ """)))UUUMMMBBB999|PP3f3333f333ff3fffff3f3f̙f3333f3333333333f3333333f3f33ff3f3f3f3333f3333333f3̙33333f333ff3ffffff3f33f3ff3f3f3ffff3fffffffff3fffffff3f̙ffff3ff333f3ff33fff33f3ff̙3f3f3333f333ff3fffff̙̙3̙f̙̙̙3f̙3f3f3333f333ff3fffff3f3f̙3ffffffffff!___wwwQtQtQtDtQtQtQtDostQJQnKmKtQJEJQtEtQKQKQQottQQtÓytÃÃÃÃÃÃÃÃÃÃÃÃÃÃÃAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAsssssst쒒쒒AÚÚÙ½AÚÚüýAÙÚÚý¼¼񼙼AÚÚÚýüüåAÚÚýýݽåååAÚÚýÚ񼼼¼񽼼åååAÚåååAÚååAÙÚüoooooAÚÙ¶oo㓔AÙÚ㔱uu޼AÚoAÚýݽAÚýÚÙ½¼AýAýÚÚÚ½AÚýÚÚÚݽAýÚýýý޼½AýÚü¼AýÚýýåAÚÚÚÙ񼼼üåååAýÚÚÚ¼½񼼼ååAÚÚåååAÚÚý½½ååAÙü񒓍AÙÚÚöAÚ¼ݽݼAÚý½޼AÚÚAÚÚAýAÚÚÚ½AÚÚýAÚýÚAÚÚ񽼼񼽼AýýÚÚ½¼½¼¼AýÚÚAÚ½AÚýÙ񒎍Aü½AÙÙ⽶޼޼AÚÚÚÚüAÚýÚÚÚåAýýýÙ½åååAýÚÚÚååAýýÚåååAÚÚÙååAÚÚýAýÚýýÚÙAÚÚ¼üAýýAÚÚ񼽼åAÚýݼååAýÚååAÚüü񽼼¼ååAÚýޓååAý񼓼½AÚÚÚAyÚÙAÓýAÚÚÚü½½¼¼AÚÚÚ񼼼½½񼼼½AÚÚÚÚA¼¼½¼½üAÚÚAÚÚښÚÚÚÚýAښÙÚÚÚýýÚAAÙÚsstssssstsssttttAÚÚÚÙAÚښÚÚÚAÚÙښÚÚÙAÚÚښÚÚÚÚÚAÚÚÚ "--&TNPP & ՜.+,D՜.+,d     Ļʾh(aĻ=h  Times New Roman _GB2312SymbolArial Wingdings 2 Wingdings ĬģȾɫԭܾøϸڵùضϸϸڵ#v6wʿռ䣨periplasmic spacePowerPoint ʾĸv7wϸȱϸ$vwϸĤ(cytoplastic membrane4. ϸĤĽṹ뻯ѧPowerPoint ʾĸPowerPoint ʾĸPowerPoint ʾĸ5. ϸĤĹܣPowerPoint ʾĸvwĤϵͳ  õ ʾĸģ õƬ 8@ _PID_HLINKSALB?http://www.slic2.wsu.edu:82/hurlbert/micro101/pages/Chap3.html1http://www.umass.edu/microbio/rasmol/cutlips.htmFhttp://info.bio.cmu.edu/Courses/BiochemMols/BuildBlocks/Membrane.htmlDhttp://intro.bio.umb.edu/111-112/111F98Lect/membranes/memblect.html?http://www.slic2.wsu.edu:82/hurlbert/micro101/pages/Chap5.html Hydrophobic?http://www.slic2.wsu.edu:82/hurlbert/micro101/pages/Chap5.html Hydrophilic;http://www.nyu.edu/pages/mathmol/library/lipids/index.html9http://esg-www.mit.edu:8001/esgbio/lm/lipids/lipids.html>http://lenti.med.umn.edu/~mwd/cell_www/chapter2/membrane.html nf_uirf[.ppt -1,2,_uirvb_` 26~̃.ppt#-1,1,YVZ8h(SO(nuclear body;nucleoid)_tŲ _i_0  !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~      !"#$%&'()*+,-./0123456789:;<=>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqstuvwxyz{|}~Root EntrydO)Pictures;Current UserSummaryInformation(rQPowerPoint Document(DocumentSummaryInformation8