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%R .!Writing Workshop #3 Results and Discussion The examples on the following slides were all excerpted from real papers These illustrate common problems that students encounter when drafting their Results and Discussion sections When reviewing each of these examples, ask yourself whether your own paper could provoke a similar criticism. How might you change your own writing to address or avoid such criticisms?>ZoZO  &Distinguish the assay from the concept'   &Distinguish the assay from the concept'   >Don t overuse personal pronouns   Avoid lab slang  Avoid lab slang  %Be wary of cryptic explanations&Be wary of cryptic explanations,More cryptic statements- More cryptic statements#Eliminate unnecessary lanes in gels$   #Eliminate unnecessary lanes in gels$   #Eliminate unnecessary lanes in gels$   BFigure legends shouldn t be lists$BFigure legends shouldn t be listsName plasmids only after you ve described their successful testingName plasmids only after you ve described their successful testingName plasmids only after you ve described their successful testingEliminate unnecessary details  Eliminate unnecessary details  Eliminate unnecessary details   Eliminate unnecessary details  Beginning the DiscussionBeginning the Discussion)Citing the references+Citing the referencesD Discussion as  True Confessions 'Ending the Discussion(Ending the Discussion ` ` ̙33` 333MMM` ff3333f` f` f` 3>?" dd@|?" dd@  " @ ` n?" dd@   @@``PR    @ ` ` p>>   $(    6\ P  T Click to edit Master title style! !  0    RClick to edit Master text styles Second level Third level Fourth level Fifth level!     S  0p ``  X*  0 `   Z*  0 `   Z*H  0޽h ? ̙33 Default Design  0$(  r  S  P   r  S   H  0޽h ? ̙33   G ? P4 ( i 4l 4 C PP   > 4 0̏  "Transcriptional Fusion Assay Analysis GUS assays were performed in order to both reveal whether or not the promoter is transcriptionally active and to measure the promoter activity in each of the different strains if it is transcriptionally active. In order to perform the GUS assays, constructs were made by ligating the putative promoters from the & gene into the expression vector pAL280.&%mb|    W    J     J    4 0E (Assaying & promoter activity To determine the activity of the & promoter in the wild type and mutant strains of AN12, we performed a GUS assay.@n   4 BHGhHԔ  I,$D 0 r&The GUS assay is a tool, not a concept'' '  B 4 BhGHԔ  _Z ,$D 0 GUS = enzyme gusA = gene6    *        4 BG HvԔ y z ,$D 0 ^This one is closer    4 BȳGeH@wԔ  Ji ,$D 0 o#But it misses the point in the text$$ $  H 4 0޽h ?O@4444 ̙33  `X` 8( '`& 8r 8 S  P   > 8 0T  "Transcriptional Fusion Assay Analysis GUS assays were performed in order to both reveal whether or not the promoter is transcriptionally active and to measure the promoter activity in each of the different strains if it is transcriptionally active. In order to perform the GUS assays, constructs were made by ligating the putative promoters from the & gene into the expression vector pAL280.&%mb|    W    J     J    8 0˟E (Assaying & promoter activity To determine the activity of the & promoter in the wild type and mutant strains of AN12, we performed a GUS assay.@n    8 s *֟E? ,$D  0 F2Assaying & promoter activity To determine the activity of the & promoter in the wild type and mutant strains of AN12, we performed a transcriptional fusion assay in which the promoter from the & gene was fused to the coding sequence of the b-glucuronidase reporter gene (gusA).nj3333333F            8 s * |,$D  0 tTranscriptional Fusion Assay Analysis Transcriptional fusion assays were performed in which the putative promoter was fused to the open reading frame of the b-glucuronidase reporter gene (gusA). Measuring GUS activity in this way would both reveal whether the promoter is transcriptionally active and measure its activity in each of the different strains. In order to perform the assays, constructs were made by ligating the putative promoters from the & gene into the expression vector pAL280.%33J333333)3 ~         P         J  H 8 0޽h ? ̙33p   p <( Vf <l < C P    < s *xE,$ 0 \To obtain a gentamicin-resistant transposome, we isolated our transposon from pMSR1 using...]]b                    < s *0[  ,$D  0 &\To obtain a gentamicin-resistant transposome, we isolated the transposon from pMSR1 using...4]:3 b                   l  =;"  <= ;",$D 0 < B GHԔ  =;,$D 0 Peek!     < BGNHԔ  =;",$D 0 Peek!   H < 0޽h ?/ < < ̙33S   @{( h @r @ S P    @ s *"E,$ 0 In order to determine if the transposome had really inserted at random into the genome, the plasmid rescues of all strains were sequenced...F     2    *   @ B*GHƹԔ U * ,$D 0 PHuh?     @ s *.D ,$D  0 In order to determine whether the transposome had really inserted at random into the genome, we examined the sequences in the genome into which the transposons had inserted. To do this, we first recovered each of the transposons along with a portion of the adjacent genomic DNA via a plasmid rescue procedure (see Materials and Methods). Sequencing the genomic DNA recovered in this manner revealed...D3@73~"     f     ;     6    p  H @ 0޽h ?@ ̙33  ~vD(  Dr D S 1P    D s *H@E,$ 0 .The plasmids were also sequenced using a forward primer for the transposome, and the upstream regions were BLAST compared for homology with known sequences.F     4     R   D BJG H3Ԕ  7 a ,$D 0 PHuh?    D BNGJ HȶԔ l#o ,$D 0 ]Upstream of what?   g D s *\R~  ,$D  0 The plasmids were also sequenced using a forward primer for the transposome, and the sequences beyond the termini of the transposons were examined via a BLAST analysis (Altschul et al., 1990) to determine whether they resembled known sequences in GenBank.(U3~     4     .     %     N  H D 0޽h ?/ DD ̙33  e]l(  lr l S % l rf^   fr^ ,$D  0_N 4,    f^    <A ??^     <A ??z,"     <jQ 51   <\jrQ 52   <bjQ 53fB   6D8} }    < ,   8~1.5 Z   s *4LZ   s * K, f   6#: f   6rO `B  0DԔ`B   0DԔ}  H  0޽h ? ̙33    D (  x  c $4P   X  0A?\ WF 4,   f^   <A ??^    <A ??z,"    <4 jQ 51  <p#jrQ 52   <&bjQ 53fB   6D8} }    <),   8~1.5 Z   s *4LZ   s * K,   6,3  ~Fig.4. Verification of S-34, S-42 via HindIII and Pst1 digestion. Lane 1 contains a 1kb DNA ladder. Lane 3 and 4 contains S-34 plasmid rescue, which shows the expected 1.5 kb band between the respective restriction enzyme sites on the transposon. Similarly, lanes 5 and 6 contain the S-42 plasmid rescue, also showing the 1.5 kb band. Multiple other bands indicate presence of multiple HindIII sites in plasmid. &"""" "A""" >%   6h;O  {Figure 4. Plasmid Rescue of S-34, S-42. Lane 1, 1kb DNA ladder. Plasmids recovered from transposants S-34 (lane 2) and S-42 (lane 3) were digested by HindIII and PstI. Note, both plasmids produced the expected 1.5 kb band derived from the transposon. Additional bands indicate presence of multiple HindIII sites in plasmid. The similarity of these two plasmids suggest that the two transposants were clonally derived.B"&3"&3""U&3""""&3"&3" &3" &3%"""^&3tX 1H 0M H  0޽h ? ̙33      d (  dr d S 8RP   x d <A ??'G  d 6S\[ h ~Figure 4. Agarose gel electrophoresis (FspI digests of in vitro pCR2.1 TOPO transformants): Lane 1: Molecular Weight Marker. Lane 2: Colony #1, PCR transposome inserted into 1.7 kb segment of TOPO. Lane 3: Colony #2, PCR transposome inserted into 1.1 kb segment of TOPO. Lane 4: Digested TOPO, expected bands at 1.0 kb, 1.1 kb, 1.7 kb. Lane 5: Colony #1, PCR transposome inserted into 1.7 kb segment of TOPO. J7"""A"t ! = < ~ ) d B`GHշԔ l>,$D 0 ]Written as a list    d B dGwH:IԔ  r ) ,$D 0 ^Lots of repetition    d BgGHF Ԕ  ),$D 0 After all this, it s not clear what main observation was supposed to beHH H    d B  P`v(  `x ` c $P    ` s *|E ,$ 0 0Purified PCR products were then excised from the gel, purified, and cloned separately into pCR2.1-TOPO (Figure 2). The appropriate colonies were selected for each insert and the plasmids were extracted by miniprep. Verification of each of these pCR2.1-TOPO constructs was carried out by DNA sequencing and by various restriction enzyme digests, as shown in Figures 3, 4 and 5. These constructs were named pTOPO_ERG12, pTOPO-ERG8, and pTOPO-MVD1, respectively, to distinguish between the genes that were cloned into each plasmid. 4z3                      P      H ` 0޽h ? ̙33  rj` ( D  x  c $P     C A\\Bionet\plessard\Project Labs\Project Lab 2003\Writing workshop 3\Caitlin before.jpg^Y/ I  BGINHlԔ  N,$D 0 jWay too many restriction sites     BGHԔ ^ ,$D 0 p$2 figures could be combined into one%% %  H  0޽h ?/    ̙33=O  NNp`d(M(   (x ( c $0P    ( C A\\Bionet\plessard\Project Labs\Project Lab 2003\Writing workshop 3\Caitlin before.jpg^Y/ I42 ( # _<j  ( 6$$} p EcoR I * 1&       ( zBCDE F5%)@  ( 6$  mXba I 5&     ( 6 $ > p Spe I * 10&        ( 6$$"q b Sal I * 14&       ( 6$VB^ p Sph I * 20&        ( zBrCDE F5%rrQ@h  ( 6L$h b Not I * 24&       ( zBLCDE F5%LL@  ( 6$ nEag I 25&      ( zB3C}DE F5%3}3@B} ( 6$ ; c Sac II * 28&      ( zBCJDE F5%J@u ( 6#$5 p Sbf I * 36&       ( zB CDE F5% @ ( 6 ($h p Pst I * 37&       ( zBCDE F5%F@ ( 6,$U c Bam HI * 42&      ( zB&CDE F5%&@ ( 6T1$! nNco I 52&      ( zB9CDE F5%99@G ( 66$T p Pvu II 397&       ( zBFCDE F5%F@ @s  ( 6$;$@( p Pvu II 490&       ( zB`CDE F5%Y`@ k ( 6?$sk p EcoR V 640&       ( zBCYDE F5%Y @qI  ( 6E$1Iv~ p Mlu I 1088&       !( zBCDE F5%@8 "( 6K$  o XhoI 1685&       #( zBC DE F5% @ 5  $( 6O$4 '  p Cla I 1777&       %( zBC:DE F5%-:@   &( 6U$   o SmaI 1959&       '( zBCfDE F5%Mf@P i  (( 6X[$ i  p Ase I 2285&       )( zBfCDE F5%Syf@ <c  *( 6a$W ~  o StuI 2709&       +( zBrCDE F5%Lr@ (i  ,( 6f$ q  o NcoI 2768&       -( zBlC DE F5%Ll @ X  .( 6l$ X<  p PvuII 2798&       /( zBMC>DE F5%MM>@ %)  0( 6Xr$) %Rv  p Mlu I 2842&       1( zB CKDE F5% K@p  |  2( 6x${ 0  o PvuI 3264&       3( zB,CDE F5%,@p h6  4( 6}$5 f  r HindIII 3472&       5( zB?CDE F5%?@@    6( 6$ 0  p Sca I 3675&       7( zBFCDE F5%F@   8( 6X$ _  p Mlu I 3869&       9( zBRCDE F5%Rf@ DxW  :( 6$7 &_  p Eag I 3974&       ;( zByCYDE F5%yY S@P   <( 6ؔ$    fEco47 III 4372&   =( zBC&DE F5%&' @ p  >( 6p$  A  p Eag I 4750&       ?( zBCDE F5%2@ pH  @( 6d$G  p Xba I 4938&       A( zBC,DE F5%, @P  B( 6$$ ] o StuI 5284&       C( zBC?DE F5%?- @ & D( 6$  o KpnI 5424&       E( zBCYDE F5%Y_ @  F( 6l$D  r HindIII 5604&       G( zBCDE F5%Y_@% H( 6,$ 2 o MluI 5622&       I( zBCDE F5%&&@e J( 6$M  p Bgl I 6046&       K( zBlCDE F5%l?@GD L( 6$ET o NcoI 6172&       M( zBLCDE F5%LL@ N( 6l$k r HindIII 6363&      2 O( BC]SENGHVJ]SQ `T /`T /]S /]Sv P( 6$" \Ptrc&  2 Q( B0RCLENG&HZJLQ .`Tx#0R|9.`Tx#0R|9Lx#0R|9L' R( 6$qE ]lacIq&  2 S( C3ENGAfH:#JQ "`TU\TDD3"`TU\TDD3\TDD37f  T( 68$ >  \KanR&  2 U( BBCENGEH%tI/%JQ y`TBCNKy`TBCNK/%BCNK/%e  V( 68$ a  ]SpecR&  2 W( BSCKENGmuH!ISJQ N`T|-KN`T|-KS|-KSi! 2 X( BSCeJENG5&vHISJQ c#`T+eJ c#`T+eJ S+eJ Sj  Y( 6$ N  `RP4 mob&    2 Z( B+TCSSENGH:I+TJSSQ qMFqMF+TSSqMF+TSSg [( 6$ mNG2 ori&     \( 6$ihl _pJP10(   ]( 6$[E  m6725 bp&     ^( 0($  Figure 5. pJP10. A plasmid of 6725 base pairs designed to express inserted genes from the trc promoter. Ptrc is an IPTG-inducible promoter. Ori is the origin of replication, which is capable of replicating in AN12. SpecR indicates spectinomycin resistance. KanR indicates kanamycin resistance. lacIq is the lac repressor gene. Restriction enzyme sites are provided for use in verification digests. An asterisk indicates a restriction enzyme that cuts the plasmid only once.t K       B    @              H                                      c( B%G_HMԔ ' t,$D 0 q%Some features labeled but not defined&& &    d( B%GZdH,Ԕ {  g ,$D 0 fSome details not necessary   H ( 0޽h ?O(Q(S(U(W(X(Z( c( d( ̙33%   "^$ (  $x $ c $< %P  %  $ C A\\Bionet\plessard\Project Labs\Project Lab 2003\Writing workshop 3\Caitlin before.jpg^Y/ I:2 $ 3 bHr   $ < %[d,  EcoR I 18       $ <%orl  Spe I 108      $ <4%_v s Sal I 148     $ <%  Sph I 208      $ <p!%/ s Not I 248     $ <t&%o t Sac II 288     $ <+%b  Pst I 378      $ <40%2 s Bam HI 428     $ <5%  Nco I 528      $ <p:% {   NcoI 27688      $ <t?%"HR  NcoI 61728     2 $ B2CXSENG&H:JXSQM `T! 29`T! 29XS! 29XS #$ <D%4" `Ptrc*  2 $$ B:RCuLENGT'H [JuLQM `Tՠ#:R9`Tՠ#:R9uL#:R9uL2 ($ <(I%rD ulacIq>  2 )$ C2ENGgH$JWQM `TU]T?D2`TU]T?D2W]T?D2WBk  -$ < N% H  `KanR*  2 .$ B"CENG|EHsI$JQM [y`T"CNK[y`T"CNK$"CNK$k  2$ <R% h*  aSpecR*  2 8$  B-TCXSENGH I-TJXSQM M GM G-TXSM G-TXSj :$ <tW% qNG2 ori*     ;$ 6h\%`S apJP10* $   <$ <h`%bL  m6725 bp&    ^B R$ 6DAl^B S$ 6D %t ^B T$ 6D5\^B U$ 6D X$ 0tp%  Figure 5. pJP10. A plasmid of 6725 base pairs designed to express inserted genes from the trc promoter. Ptrc is an IPTG-inducible promoter. Ori is the origin of replication, which is capable of replicating in AN12. SpecR indicates spectinomycin resistance. KanR indicates kanamycin resistance. lacIq is the lac repressor gene. Restriction enzyme sites are provided for use in verification digests. An asterisk indicates a restriction enzyme that cuts the plasmid only once.t K       B    @              H                                      ]$ Bw%GHokԔ @ c ,$D 0 `Redundant with image    ^$ Bz%GH~Ԕ   q ,$D 0 l Could be written more succinctly!! !  H $ 0޽h ?p$$$)$.$ 8$]$^$ ̙33   %,( # ,x , c ${%P  %  , C A\\Bionet\plessard\Project Labs\Project Lab 2003\Writing workshop 3\Caitlin before.jpg^Y/ I:2 , 3 bHr  , <%[d,  EcoR I 18      , <%orl  Spe I 108      , <%_v s Sal I 148      , <%  Sph I 208       , < %/ s Not I 248      , <%o t Sac II 288      , <̡%b  Pst I 378       , <Ц%2 s Bam HI 428     , <$%  Nco I 528      , < % {   NcoI 27688      , <%"HR  NcoI 61728     2 , B2CXSENG&H:JXSQM `T! 29`T! 29XS! 29XS , <d%4" rPtrc<  2 , B:RCuLENGT'H [JuLQM `Tՠ#:R9`Tՠ#:R9uL#:R9uL2 , <%rD ulacIq>  2 , C2ENGgH$JWQM `TU]T?D2`TU]T?D2W]T?D2WBk  , <% H  `KanR*  2 , B"CENG|EHsI$JQM [y`T"CNK[y`T"CNK$"CNK$k  , <P% h*  aSpecR*  2 ,  B-TCXSENGH I-TJXSQM M GM G-TXSM G-TXSj , <% qNG2 ori*     , 6%`S apJP10* $   , <,%bL  m6725 bp&    ^B , 6DAl^B  , 6D %t ^B !, 6D5\^B ", 6DL #, 0,%  Figure 5. pJP10 expresses inserted genes from the IPTG-inducible trc promoter (Ptrc). NG2 ori, origin of replication, capable of replicating in AN12; SpecR, spectinomycin resistance marker; KanR, kanamycin resistance marker; lacIq, lac repressorA                A             :                             H , 0޽h ?_P,,,,, ̙33  WO P(  Pr P S oP    P s *\pE,$ 0 Discussion The sequence deviation of pFRO is not surprising because the shotgun sequencing method that was used to sequence the genome has potential holes.& *%    r  & P Bt|GT HԔ %,$D 0 4Jumps right into the data&    * P B|GHTԔ d 0,$D 0 8On a negative note, no less&    H P 0޽h ?/ PP ̙33!     @TI (  Tx T c $LP    T s * SE?,$ 0 f Discussion     z T s *U,$D  0 While many eukaryotes produce isoprenoids via mevalonate, very few prokaryotes use this pathway, the non-mevalonate pathway being much more common. Therefore it is not surprising to find genes encoding the entire enzymatic complement for the non-mevalonate pathway in the bacterium we studied. What is peculiar, though, is the presence of a gene encoding HMG-CoA reductase. In other organisms, this enzyme constitutes the first committed step toward isoprenoid biosynthesis via the mevalonate pathway, and the enzyme is rarely encountered in any other context. In this project we sought to determine the role of HMG-CoA reductase in this strain. We cloned and sequenced the HMG-CoA reductase gene from the bacterrial chromosome and found a small number of sequence discrepencies relative to that reported in the genome database. This sequence deviation is not surprising because& 8vF3/3                 1          g         O          }    1              0     h   T BxnG H'Ԕ 1 > e,$D 0 m!Start by restating the hypothesis"" "  H T 0޽h ?T ̙33h     | (  |x | c $%P  %  | s *&w,$ 0 22The location of the ptsH promoter is unknown, if there is a promoter for ptsH in Rhodococcus. In similar bacteria, such as Streptococcus salivarius, Shine delgarno sequences have been found upstream of the ptsH gene (Gagnon et al. 1993). Two carbon source regulated promoters for ptsH in Streptomyces coelicolor have also been found (Nothaft et al. 2003). Furthermore, promoters are normally found within& 1  ;Ga    0    <          *    F            B  D | B&G=H Ԕ B ,$D 0 RAnd from this example we ve learned& what?** *   | B&GYHݪԔ  j ,$D 0 Wait! You re onto a 2nd topic and I still don t understand the 1st.VD   )    D  H | 0޽h ?/ || ̙33  H(  x  c $%P  %   s *@$&w,$ 0 22The location of the ptsH promoter is unknown, if there is a promoter for ptsH in Rhodococcus. In similar bacteria, such as Streptococcus salivarius, Shine delgarno sequences have been found upstream of the ptsH gene (Gagnon et al. 1993). Two carbon source regulated promoters for ptsH in Streptomyces coelicolor have also been found (Nothaft et al. 2003). Furthermore, promoters are normally found within& 1  ;Ga    0    <          *    F            B    s *Q&p,$D  0 :f& In similar bacteria, such as Streptococcus salivarius, Shine Delgarno sequences have been found upstream of the ptsH gene (Gagnon et al., 1993), which enabled these researchers to identify the location of the ptsH promoter in that species. A similar strategy would be helpful for identifying the location of the ptsH promoter in Rhodococcus, had such a consensus sequence already been identified. Two carbon source regulated promoters for ptsH in Streptomyces coelicolor have also been found (Nothaft et al., 2003). The more proximal of these two promoters was constitutively expressed, whereas the distal promoter was strongly induced by glucose. This illustrates the possibility that& 323C33d33 3 383+3 3 ,         +    ]    d    z                    H  0޽h ? ̙33\     Lt (  Lr L S C&P  &  L s *D&E,$ 0 <The transformation rate for B264-1 is almost so low as to be useless for the purposes of generating mutations. Given that in three months and as many different preparations of competent cells we only generated 3 transformants& *        L s *c& ,$D  0 64Given how little is known about the mechanism of conjugal transfer between rhodococci, any progress in this field would be welcomed. Rhodococcus sp. B264-1 has the ability to transfer DNA to other Rhodococcus strains, and it is reasonable to suspect that the genes required for this activity lie on one of the two megaplasmids that reside within B264-1. While it is clear that there is still much work to do, we have taken the first steps toward genetically tagging the elements required for conjugal transfer in Rhodococcus sp. B264-1& 3 33303 323 3 3*J         L Bd&GHԔ ,$D 0 f Oooh, harsh!         L B&&GzPHԔ |H x ,$D 0 jSuch a tragedy&    H L 0޽h ?/ LL ̙33.  tF(  tr t S p|&P  &  t s *}&E,$ 0 l& Another possible explanation for the knockout growth is that over longer periods, quinones and other metabolic byproducts have diffused from the KY1 side of the plate to the 50A2 side (Figure 3c) and the cells are able to metabolize these, if poorly.*S        t B&GhH"Ԕ  ,$D 0 SThe End    t Bl&GHԔ 8  _ ,$D 0 Ending with this comment makes it seem as though this issue of quinone metabolism was the most important conclusion of the research *?    =  H t 0޽h ?/ tt ̙33  OGx(  xx x c $@&P  &  x s *&E,$ 0 l& Another possible explanation for the knockout growth is that over longer periods, quinones and other metabolic byproducts have diffused from the KY1 side of the plate to the 50A2 side (Figure 3c) and the cells are able to metabolize these, if poorly.*S        x s *& ,$D  0 The results we have obtained to date argue in favor of the hypothesis that nimB encodes a function that is critical for naphthalene metabolism in Rhodococcus sp. KY1. However, it is also clear that more work will be needed to confirm the precise role of this gene as well as that of the neighboring gene, ORF5468. 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