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mcrb 265 > functional morphology of prokaryotes > Flashcards

functional morphology of prokaryotes Flashcards

1
Q

2 major structural differences between prok and euk

A
  1. prok have no defined organelles.

2. prok are generally much smaller in size.

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2
Q

structure of prok

A

simpler than eul.

nucleoid, not bound. sometimes have plasmid, have cell wall.

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3
Q

structure of euk

A

sometimes have cell wall depending on euk.

have ER, golgi, mt and true nucleus

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4
Q

how S/V ratio affects prok growth

A

larger SA/V ratio = outside interacting with more of enviro, more nutrients + greater concentration gradient.

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5
Q

why do euk want to be bigger w smaller s/v ratio?

A

eat other smaller cells, more complex + specialized. sacrifice growth for increased complexity.

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6
Q

what constrains sie of prok?

A

ribosomes = can be as small as few proteins, cell membrane + at least 1 ribosome. but need these 3 to function + be called bacteria.

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7
Q

morphologies of prok cells

A

coccus, rod, spirillum, filamentous, stalk, hypha, spirochete

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8
Q

spirochetes : 2 ex organisms

A 
treponema pallidum (syphilis) + borrelia burgdorferi (lyme disease)
-> drill into muscle cells + cause disease
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9
Q

vibrio - bent rod. ex organism?

A

vibrio cholerae = diarrhea

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10
Q

cocci, cluster or pair or chain or tetrad

A

cluster = staphylo, pais = diplo. chain = strepto. tetrad = sarcina

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11
Q

appendaged/budding

A

growth stalk attaches to surface.. or bud - pillus cell buds off until settles somewhere else.

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12
Q

filamentous

A

chloroflexus: photosynthetic, ancient

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13
Q

define monomorphic

A

one shape, observed in pure cultures

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14
Q

define pleomorphic

A

multiple shapes.

-chage during growth. response to enviro cues: sporulation (nutrient limitation)

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15
Q

example of pleomorphic organism?

A

arthrobacter sp. morphogenesis from rod to coccus during growth3

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16
Q

macromolecules in prokaryotes

A

protein. nucleic acid (dna in nucleiod; rna in cytoplasm), polysacch: cell wall + storage. lipids = cytoplasmic membrane, cell wall, storage

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17
Q

permeability barrier

A

prevent leakage + transport of nutrients in + out

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18
Q

protein anchor in bacterial membrane

A

site of proteins involved in transport, bioenergetics + chemotaxis anchored to function externally

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19
Q

three functions of bacterial membrane

A

permeabiltiy barrier, protein anchor, energy conservation

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20
Q

energy conservation in bacterial membrane

A

generation + use of pmf

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21
Q

membrane chemistry = ester vs ether

A

ester = bacteria + eukarya.

ether : archaea = isoprene chain, more complex + stable

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22
Q

archaea - monolayer vs bilayer

A 
bilayer = two shorter chains. hydrophobic inside, hydrophilic inside. 
monolayer = one long chain with 2 hydrophilic parts. must move in one piece = harder to move
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23
Q

function of hopanoids?

A

rigidity to otherwise flexible membrane due to planar configuration

euk: cholesterol (three 6-memer, 1 5-member)
bacteria: diploptene (four 6-member, 1 5-member)

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24
Q

rate of transport for water, uncharged non-polar, charged non-polar

A

excellent; uncharged: fair; charged = extremely poor.

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25
Q

transporters require energy = what is energy used?

A

proton motive force to generate ATP.

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26
Q

what is simple transport?

A

driven by energy in porton motive force

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27
Q

what is group translocation?

A

chemical modification of the transported substance driven by phosphoenolpyruvate.

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28
Q

The ABC system: periplasmic binding proteins are involved and energy comes from ATP

A

periplasmic binding proteins are involved and energy comes from ATP.

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29
Q

three mechanisms of simple transport driven by PMF

A

uniporter, antiporter, symporter

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30
Q

group translocation - ex: the phosphotransferase system

A

glucose interacts with E2c. signal to begin phosphorylation process. E2c change in conformaiton = change in e2b -> e2a. once e2a conformation change, interact with HPR = attracts enz 1. enz 1 hydrolyzes PEP -> pyruvate and carries Pi across back to E2c where Pi added to glucose + complex carried across membrane

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31
Q

ABC (ATP -binding cassette) transport.

- which bacteria? why?

A

only in g(-) bacteria.
occurs in periplasmic space. in g(-) because have larger ppspace. molecule binds to specific binding protein = complex; attaches to membrane-spanning transporter. ATP hydrolysis leads molecule to shift thru transporter

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32
Q

transport across the membrane = limited why?

A

carrier saturation. max growth rate, or all transporters full.

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33
Q

who made gram stain? what is procedure?

A

christian gram.
1. stain with violet-iodine. binds to membrane.
in g(+): goes thru pg layer = no leaking when washed.
cells decolorized with alcohol: g+ dehydrated - prevent escape of purple dye.
3. counter stain with safranin - pink = g(-)

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34
Q

important physiological differences btw g(+) and g(-) bacteria

A
  • g(+) more susceptible to b-lactam.
    +: in spore form more resistant to heat + mechanical stress.
    + require additional vitamins or AA for growth
    g(-) more widespread.
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35
Q

how PG is made?

A

glycan = NAM + NAG disaccharides bonded by b(1,4) glycosidic bonds.

  • > AA link to NAM. L - Alanine; D-glutamic acid; d-alanine, meso-diamino-pimelic acid (allows resistance to peptidase)
  • significant that there’s D-aa. everywhere else there is :-aa.
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36
Q

PG in g+

-> connection?

A

l-ala; d-glut; l-lysine; d-ala.

peptide interbridge: 5 glycine. why? bc opposite handedness from L-lys to d- ala

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37
Q

pg in g(-)

A

l-ala; d-glutamic acid; meso-diaminomietic acid; d-ala

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38
Q

why strong structure in PG?

A

strong btw inter-linkage. also strong between sheets = bonds to strengthen.

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39
Q

2 main inhibitors in cell wall biosynthesis

A

lysozyme hydrolyzes b(1,4) glycosidic bond. growing + present bacteria
2. penicillin blocks transpeptidase that connects (DAP to D-ala) 2-glycan- linked peptide chains together. only hits growing bacteria

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40
Q

cell in lysozyme + sucrose solution ?

A

protoplast = bacteria without cell wall. cel wall digested

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41
Q

pseudoPG in some methanogenix archaea

A

b(1-3) linkage btw NAG and NAT prevent lysozyme attack.

not sensitive to lysozyme bc lysozyme hits b(1-4) resistant to penicillin = why? bc diff arrangement of aa in chain.

42
Q

achaeal cell envelopes

A

without: cw, cm, cell plasma.
with: s-layer: bound by trans-membrane protein. proteinaceous on outside. space between s-layer and CM. similar stability + structure that CW and pseudo PG have.

43
Q

g+ : what is teichoic acid?

A

component of Cw that gives flexibility. extends surface of cw , gives it negative charge.

lipoteichoic acis links cw + cm

44
Q

g- cw: components?

A

cm - has TM protein in peiplasmic space.
PG - has lipoproteins that connect cw with outer membrane.
polysacchs on outer membrane interact with outside world. lipopolysacchs have lipid a core, core polysacch and o-polysachh. o-polysacch changes

45
Q

lipopolysacchs of g- cw.

important

A

barrier agsint host defenses. lipid A = endotoxin to animals; reason for pathogenicity. o-specific polysacch varies.
order: lipid A (anchor to membrane) -> letodeoxyoctonate -> core -> o-specific (specific to particular chain)

46
Q

what is a porin?

A

channel for entrance + exit of hydrophilic low molecular weight (<00daltons) substances (ie. water, ions) no proteins, large molecules

47
Q

what’s in periplasmic space

A

enxymes that participate in nutrient acquisition + metabolism.
- small, essentially non-existent in g+. (bc cw bound to cm

48
Q

chemolithotrophs - pp space

A

have extensive arras of e- transport proteins extending to outer membrane for uptake + metabolism of inorganic ions. oxidize toxic chemicals b enzymes in ppspace linked to outer membrane

49
Q

g+ bacteria: exoenzymes?

A

secreted by cell to aid in transporting nutrients.

50
Q

capsule + slime

A

produced by cell in organic rich enviro.
capsule/slime act as energy storage + protect against enviro, dehydration + organic material. = increase survival attachment + virulence.

51
Q

one way to visualize capsule/slime

A

india ink - negative stain bc doesn’t penetrate capsule. everything but capule stained.

52
Q

4 types of cellular inclusions

A
  1. carbon storage
  2. sulfur storage
  3. magnetosomes
  4. gas vesicles
53
Q

function of carbon storage cell inclusion?

A

store carbon in different forms until needed.

bacteria + archaea

54
Q

function of sulfur storage

A

sulfur granules stored for low sulfide consitions. some organisms use sulfide for ox-phos

55
Q

function of magnetosomes

A

allow bacteria to orient + migrate along geomagnetic fields; usually associated with O2 concentrations.

56
Q

function of gas vesicles

A

important for aquatic microorganisms. allows them to float in large colonies - buoyant.
float during day to get light, sink to bottom at night to feed

57
Q

endospores - when do they occur? triggered when? g+ or -?

A

occurs as bacteria age due to nutrient deprivation. tigger is nutrient, not enviro stress.
all spore-forming are g+, but not all g+ are spore-formers.

58
Q

endospore structure - 4 layers

A

spore coat; cortex; exosporium; core wall. = dehydrated, resistant to degradation

59
Q

difference btw endospore + exospore

A 
endo = formed inside cell. repackage DNA + pop out of vegetative cell
exo = daughter cell is sport = ejected
60
Q

what is dipicolinic acid?

READ IN TEXTBOOOK

A

aka DPA. - nitrogenous ring w carboxylic groups, charged.
unique to bacterial spores.
-> 10% dry weight of endospores.
-> high in calcium ion, crosslinks DPA
-> rigid structure. less availability for water - decreases damage to DNA + cell

61
Q

shapes of endospores

A

central
subterminal
terminal bacillus: aerobic g+
terminal clostridium: anaerobic g+

62
Q

ways in which endospores return to vegetative state

A
  1. heat endospore
  2. nutrient broth
  3. germination is rapid, synthesizes + breaks open spore coat.
63
Q

pili - function?

A

form conjugation bridge between bacterial cells for transferring DNA and attach to host cells
-pillus formation depends on plasmid present.

64
Q

types of flagella in bacteria

know this

A
  • attached at one end.
  • attached at both ends
  • tuft at one end
  • all around surface.
65
Q

flagellum of g- bacteria - components

A

filament - flagellin.
hook - hook protein
basal body - 4 rings : L ring, P ring, MS ring, C ring.
motprotien around MS + C rings fli protein between MS and C rings

66
Q

flagellum g-: function

A

pmf thru mot protein causes it to spin. interacts with Fli protein and causes it to spin in turn with MS ring.MS ring hold central column which turns too.p-ring allows column to go through. l-ring spans uter membrane. maintains structure + holds column in place.

hook area is where flagellin filament grows. proteins flow thru hollow column to end of hook

67
Q

how pmf causes mot protein to move

A

ms and c-rings are charged. when H+ moves thru, electrostatic repulsion forces MOT protein to spin.

68
Q

development of flagellum - g-

A

MS ring assembled in CM. ; P-ring forms in periplasm.; L-ring froms in LPS.; hook + cap (stops hook from forming, allows filament synthesis); flagellin thru hollow column to hook to form filament.

69
Q

difference from g- to g+ flagellum.

A

no LPS, no outer mem.

only rights.

70
Q

archaellum - contrast to flagellum

A

half the diameter; more by rotation. filament protein unrelated to bacterial. use ATP instead of pmf. FLAX protein hydrolyzes ATP causing spin of FLAX + FLAI structurally similar to Type 4 pilus.

71
Q

what is type 4 pillus

A

pokes hole in CM and injects toxin, DNA etc.

diff mechanism than flagellum,, but similar function.

72
Q

gliding motility - what organism?

A

flavobacterium johnsoniae.
-> driven by PMF.
protins in outer membrane move opposite to cell. outer mem attached to cm proteins, . again opposite motion. cm same direction as cell movement

73
Q

axial filaments - where found?

A

endoflagella; found in spirochaetes. flagella is inside body, anchored at end of cell. drills + burrows into thiings by rotation of whole cell.

74
Q

chemotaxis - what is it?

A

random cell movement in absence of attractant; attractant causes directed movement up-gradient.
by run-and-tumble method. flagella come together to push in one direction, disassemble, random motion to re-align. then run again.

75
Q

petrichous movement- what is it?

read in textbook

A

all flagella rotate counterclockwise in a bundle.

when apart, reverse direction pulls apart - FLI protein changes direction

76
Q

polar flagella - how do they work?

A

change direction by reversing rotation.

  • polar reversible: ccw forward, cw backward.
  • polar unidirectional: cw forward. stop, realign, cw forward
77
Q

when u put capillary tube full of chemical in bacterial suspension - why is there saturation?

A

saturation of distance away bc only so far they can move toward or away from.

78
Q

what is phototaxis

A

photosynthetic bacteria accumulate at wavelength where pigments abosrb.

79
Q

one nutrient that’s limited + limiting?

A

Nitrogen.

80
Q

Why is nitrogen limited?

A

bacteria can sequentially reduce nitrite into N-gas = lose nitrogen.

81
Q

function of NO in organism?

A

toxic to other organisms.

82
Q

potent greenhouse gas produced as result of denitrification?

A

N2O

83
Q

discuss anaerobic respiration

A

dont use O2 as terminal e- acceptor.
because of this, less electropositive terminal acceptor is used, such as No3-. less energy is generated bc of a worse e- acceptor.

84
Q

what organisms do anaerobic respiration?

A

prokaryotes

  • > obligate anaerobes : cannot respire with O2
  • > facultative aerobes: can respire with or without O2.

chemoorganotrophs + chemolithotrophs

85
Q

how nitrate reduction is mediated through the cell

A

e- pass thru complex1 -> Fe-S -> Q -> cyt b (NOT C). fewer ATP produced at nitrate reductase

86
Q

how denitrification is mediated through the cell

A

c1 -> Fe-S -> Q -> cyt b -> nitrate reductase (not cyt C), other cytochromes -> NO reductase.

*if continue to complete denitrificaiton = greater H+ graident + more ATP produced. costly on space in the membrane, and in genome. facultative usually stop of NO3 reductase. obligate anaerobes commit to whole denitrification process.

87
Q

sulfate reduction

  • > length?
  • > what organisms use?
A

sulfate reducing ETC is short bc fewer ATP result from it.

-> sulfidogens + obligate anaerobes use

88
Q

two major roles of TCA cycle

A

glucose respiration coupled to energy conservation + biosynthesis of key metabolites

89
Q

define anapleurotic

A

used in both catabolism + anabolism

90
Q

two problems with substrate-level phosphorylation

A

1 atp /2 gluose.

2 need to regenerate NAD+

91
Q

phenol

A

disrupt h-bonding in protein. -> disinfect

92
Q

alcohol

A

disrupt h-bond in protein and dissolve membrane lipids.

-> disinfect, antispetic

93
Q

halogen

A

oxidize cell constituents. disinfect + antiseptic.

94
Q

heavy metals

A

inactivate proteins - antiseptic

95
Q

aldehyde + lactone

A

inactivate proteins.

96
Q

sterilizing gases

A

bind to protein.

97
Q

vapour-phase h2o2 + quaternary ammonium

A

disrupt biological membranes.

98
Q

phenol

A

h-bond to denature protein - disinfect

99
Q

alcohol

A

h-bond to denature protein + dissolve membrane -> anitseptic + disinfectant

100
Q

halogen

A

oxidize ell constituent

mcrb 265 (14 decks)

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