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Subject: =?utf-8?Q?Sign=20Up=20For=20Free=3A=20The=20evolution=20of=20carbon=20fixation=3A=20Studying=20Form=20I=20Rubisco=20using=20ancestral=20sequence=20reconstruction=20and=20mass=20photometry?=
From: =?utf-8?Q?Labroots=20for=20Refeyn?= <info@labroots.com>
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To: <gerald.wahome@saraya.world>
Date: Thu, 10 Nov 2022 16:34:23 +0000
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Free Webinar - Register Today!

View this email in your browser (https://mailchi.mp/labroots/discovering-u=
nforeseen-protein-assemblies-with-mass-photometry-229522?e=3D421d0bfc01)
https://www.labroots.com/ms/webinar/evolution-carbon-fixation-studying-for=
m-rubisco-using-ancestral-sequence-reconstruction-mass-photome?campaign=3D=
lremail

** The evolution of carbon fixation: Studying Form I Rubisco using ancestr=
al sequence reconstruction and mass photometry
------------------------------------------------------------

C.E. Credits: P.A.C.E. CE =EF=BD=9C Florida CE (https://www.labroots.com/m=
s/webinar/evolution-carbon-fixation-studying-form-rubisco-using-ancestral-=
sequence-reconstruction-mass-photome?campaign=3Dlremail)

November 17=2C 2022 | 8:00am (PST)=2C 11:00am (EST)=2C 5:00pm (CET)  https=
://www.labroots.com/intercall/add-to-calendar/Webinar/7723?start-date=3D20=
221117T080000&end-date=3D20221117T090000&TZID=3DAmerica/Los_Angeles
Register for Free (https://www.labroots.com/ms/webinar/evolution-carbon-fi=
xation-studying-form-rubisco-using-ancestral-sequence-reconstruction-mass-=
photome?campaign=3Dlremail)

=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=
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=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D=3D

Abstract
Up to now=2C the evolutionary trajectory of the most prevalent CO2-fixing=
 enzyme =E2=80=93 Rubisco Form I=2C has been difficult to study. The Rubis=
co found in today=E2=80=99s plants and algae has 8 small subunits (SSU) th=
at are absent from its ancestral form. The SSU has become essential for th=
e enzyme=E2=80=99s solubility and activity=2C hindering biochemical studie=
s into its influence on Rubisco. Our research aimed to decipher how the ob=
ligate interaction between Rubisco and its SSU evolved. This includes iden=
tifying the functional implications of Rubisco interacting with the SSU=2C=
 discovering why the modern Rubisco depends on the SSU=2C as well as how t=
he SSU modulated the evolutionary trajectories available to Rubisco. To ad=
dress these questions=2C we combined ancestral sequence reconstruction and=
 mass photometry. We re-created a long-extinct evolutionary precursor of m=
odern Rubiscos=2C which interacts with the SSU but does not depend on it.=
 With this intermediate=2C we show that Rubisco increased its specificity=
 and
carboxylation efficiency through the gain of a new accessory subunit befor=
e atmospheric oxygen was present.

Mass photometry enabled us to narrow down the evolutionary interval over w=
hich Rubisco=E2=80=99s oligomerization state changed. It also made it poss=
ible to screen for the substitutions that caused Rubisco=E2=80=99s depende=
nce on the SSU for solubility.

We show that the current form of Rubisco evolved from an octamer of large=
 subunits that started to interact with the SSU more than 2.5 billion year=
s ago. Immediately upon recruitment=2C the SSU improved Rubiscos catalysis=
 and specificity. Then=2C a substitution made Rubisco dependent on the SSU=
 for solubility. Our work sheds light on the emergence of an adaptation to=
 rising ambient oxygen levels=2C provides a template for investigating the=
 function of interactions that have remained elusive because of their esse=
ntiality=2C and sheds new light on the determinants of specificity in Rubi=
sco.

Learning Objectives
* To explain how a protein-protein interaction can re-shape the sequence s=
pace that is available to a protein during its evolution.
* To understand why hetero-oligomeric proteins start to depend on their in=
teraction partners over the course of evolution.
* To learn how mass photometry can be used to re-trace the emergence of a=
 protein-protein interaction.
* To understand how a small protein with no obvious link to catalysis can=
 influence the function of an enzyme.

** Register now (https://www.labroots.com/ms/webinar/evolution-carbon-fixa=
tion-studying-form-rubisco-using-ancestral-sequence-reconstruction-mass-ph=
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on+fixation%3A+Studying+Form+I+Rubisco+using+ancestral+sequence+reconstruc=
tion+and+mass+photometry)

Can't attend live? ** Click here (https://www.labroots.com/ms/webinar/evol=
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 exactly;-ms-text-size-adjust: 100%;-webkit-text-size-adjust: 100%;backgro=
und-color: #ffffff;background-image: none;background-repeat: no-repeat;bac=
kground-position: center;background-size: cover;border-top: 0;border-botto=
m: 0;padding-top: 9px;padding-bottom: 0;"><table border=3D"0" cellpadding=
=3D"0" cellspacing=3D"0" width=3D"100%" class=3D"mcnTextBlock" style=3D"mi=
n-width: 100%;border-collapse: collapse;mso-table-lspace: 0pt;mso-table-rs=
pace: 0pt;-ms-text-size-adjust: 100%;-webkit-text-size-adjust: 100%;">
    <tbody class=3D"mcnTextBlockOuter">
        <tr>
            <td valign=3D"top" class=3D"mcnTextBlockInner" style=3D"paddin=
g-top: 9px;mso-line-height-rule: exactly;-ms-text-size-adjust: 100%;-webki=
t-text-size-adjust: 100%;">
              =09
=09=09=09
=09=09=09=09
                <table align=3D"left" border=3D"0" cellpadding=3D"0" cells=
pacing=3D"0" style=3D"max-width: 100%;min-width: 100%;border-collapse: col=
lapse;mso-table-lspace: 0pt;mso-table-rspace: 0pt;-ms-text-size-adjust: 10=
0%;-webkit-text-size-adjust: 100%;" width=3D"100%" class=3D"mcnTextContent=
Container">
                    <tbody><tr>

<h1 style=3D"display: block;margin: 0;padding:=
 0;color: #333333;font-family: Helvetica;font-size: 24px;font-style: norma=
l;font-weight: normal;line-height: 125%;letter-spacing: normal;text-align:=
 left;">The evolution of carbon fixation: Studying Form I Rubisco using an=
cestral sequence reconstruction and mass photometry</h1>

<p style=3D"text-align: left;margin: 10px 0;padding: 0;mso-line-height-rul=
e: exactly;-ms-text-size-adjust: 100%;-webkit-text-size-adjust: 100%;color=
: #555555;font-family: Helvetica;font-size: 13px;line-height: 150%;"><span=
 style=3D"font-size:15px"><span style=3D"color:#18345D"><strong>November 1=
7=2C 2022</strong></span><span style=3D"color:#7AC243"><strong>&nbsp;</str=
ong></span></span><span style=3D"font-size:16px">|</span><span style=3D"fo=
nt-size:18px">&nbsp;</span><span style=3D"font-size:15px">8:00am (PST)=2C=
 11:00am (EST)=2C 5:00pm (CET)&nbsp;<span style=3D"color:#7AC243"><strong>=
&nbsp;</strong></span><a href=3D"https://labroots.us7.list-manage.com/trac=
k/click?u=3D6f39393ef38fb324428ff8c2c&id=3D560456b5b4&e=3D421d0bfc01" tar=
get=3D"_blank" style=3D"mso-line-height-rule: exactly;-ms-text-size-adjust=
: 100%;-webkit-text-size-adjust: 100%;color: #1e8ae7;font-weight: normal;t=
ext-decoration: underline;"><img data-file-id=3D"42943" height=3D"13" src=
=3D"https://gallery.mailchimp.com/6f39393ef38fb324428ff8c2c/images/b9d0b3b=
5-66ac-4b86-857f-08e5d0e67a46.png" style=3D"border: 0px;width: 20px;height=
: 13px;margin: 0px;outline: none;text-decoration: none;-ms-interpolation-m=
ode: bicubic;" width=3D"20"></a></span></p>

</td>
                    </tr>
                </tbody></table>
=09=09=09=09

<p style=3D"font-size: 14px;text-align: left;m=
argin: 10px 0;padding: 0;mso-line-height-rule: exactly;-ms-text-size-adjus=
t: 100%;-webkit-text-size-adjust: 100%;color: #555555;font-family: Helveti=
ca;line-height: 150%;"><span style=3D"font-family:arial=2Chelvetica neue=
=2Chelvetica=2Csans-serif"><span style=3D"font-size:14px"><strong>Abstract=
</strong></span></span></p>
<span style=3D"font-family:arial=2Chelvetica neue=2Chelvetica=2Csans-serif=
"><span style=3D"font-size:14px">Up to now=2C the evolutionary trajectory=
 of the most prevalent CO2-fixing enzyme =E2=80=93 Rubisco Form I=2C has b=
een difficult to study. The Rubisco found in today=E2=80=99s plants and al=
gae has 8 small subunits (SSU) that are absent from its ancestral form. Th=
e SSU has become essential for the enzyme=E2=80=99s solubility and activit=
y=2C hindering biochemical studies into its influence on Rubisco. Our rese=
arch aimed to decipher how the obligate interaction between Rubisco and it=
s SSU evolved. This includes identifying the functional implications of Ru=
bisco interacting with the SSU=2C discovering why the modern Rubisco depen=
ds on the SSU=2C as well as how the SSU modulated the evolutionary traject=
ories available to Rubisco. To address these questions=2C we combined ance=
stral sequence reconstruction and mass photometry. We re-created a long-ex=
tinct evolutionary precursor of modern Rubiscos=2C which interacts with th=
e SSU but does not depend on it. With this intermediate=2C we show that Ru=
bisco increased its specificity and carboxylation efficiency through the g=
ain of a new accessory subunit before atmospheric oxygen was present.<br>
<br>
Mass photometry enabled us to narrow down the evolutionary interval over w=
hich Rubisco=E2=80=99s oligomerization state changed. It also made it poss=
ible to screen for the substitutions that caused Rubisco=E2=80=99s depende=
nce on the SSU for solubility.<br>
<br>
We show that the current form of Rubisco evolved from an octamer of large=
 subunits that started to interact with the SSU more than 2.5 billion year=
s ago. Immediately upon recruitment=2C the SSU improved Rubiscos catalysis=
 and specificity. Then=2C a substitution made Rubisco dependent on the SSU=
 for solubility. Our work sheds light on the emergence of an adaptation to=
 rising ambient oxygen levels=2C provides a template for investigating the=
 function of interactions that have remained elusive because of their esse=
ntiality=2C and sheds new light on the determinants of specificity in Rubi=
sco.<br>
&nbsp;<br>
<strong>Learning Objectives</strong></span></span>

<ul>
=09<li style=3D"mso-line-height-rule: exactly;-ms-text-size-adjust: 100%;-=
webkit-text-size-adjust: 100%;"><span style=3D"font-family:arial=2Chelveti=
ca neue=2Chelvetica=2Csans-serif"><span style=3D"font-size:14px">To explai=
n how a protein-protein interaction can re-shape the sequence space that i=
s available to a protein during its evolution.</span></span></li>
=09<li style=3D"mso-line-height-rule: exactly;-ms-text-size-adjust: 100%;-=
webkit-text-size-adjust: 100%;"><span style=3D"font-family:arial=2Chelveti=
ca neue=2Chelvetica=2Csans-serif"><span style=3D"font-size:14px">To unders=
tand why hetero-oligomeric proteins start to depend on their interaction p=
artners over the course of evolution.</span></span></li>
=09<li style=3D"mso-line-height-rule: exactly;-ms-text-size-adjust: 100%;-=
webkit-text-size-adjust: 100%;"><span style=3D"font-family:arial=2Chelveti=
ca neue=2Chelvetica=2Csans-serif"><span style=3D"font-size:14px">To learn=
 how mass photometry can be used to re-trace the emergence of a protein-pr=
otein interaction.</span></span></li>
=09<li style=3D"mso-line-height-rule: exactly;-ms-text-size-adjust: 100%;-=
webkit-text-size-adjust: 100%;"><span style=3D"font-family:arial=2Chelveti=
ca neue=2Chelvetica=2Csans-serif"><span style=3D"font-size:14px">To unders=
tand how a small protein with no obvious link to catalysis can influence t=
he function of an enzyme.</span></span></li>
</ul>

</td>
                    </tr>
                </tbody></table>
=09=09=09=09

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