Human Physiology, 14th edition (2016)

(Tina Sui) #1
Cell Structure and Genetic Control 71

including gene activation and inactivation. Other proteins
modify the activity of particular enzymes, and so help to regu-
late the cell. Examples of such regulatory proteins include the
cyclins, which help control the cell cycle (see fig. 3.25 ).
Because proteins have so many important functions, the
processes of genetic transcription and translation have to be
physiologically regulated. Hormones and other chemical
signals can turn specific genes on or off, regulating protein
synthesis. However, for critically important proteins, tighter
control is required. Regulatory proteins are rapidly degraded
(hydrolyzed, or digested), quickly ending their effects so that
other proteins can produce new actions. This affords a much
tighter control of specific regulatory proteins than would be
possible if they persisted longer and only their synthesis was
regulated.
Protease enzymes (those that digest proteins) located in
the lysosomes digest many types of cellular proteins. In recent
years, however, scientists learned that critical regulatory pro-
teins are also degraded outside of lysosomes in a process that
requires cellular energy (ATP). In this process, the regulatory

Figure 3.21 The translation of messenger RNA (mRNA). (1) The anticodon of an aminoacyl-tRNA bonds with a codon on
the mRNA, so that the specific amino acid it carries can form a peptide bond with the last amino acid of a growing polypeptide. (2) The
tRNA that brought the next-to-last amino acid dissociates from the mRNA, so that the growing polypeptide is attached to only the last
tRNA. (3) Another tRNA carrying another amino acid will bond to the next codon in the mRNA, so that this amino acid will be at the new
growing end of the polypeptide.

Codons

Codons
mRNA

A

B

C

D

E

F

G

H

I

tRNA
4

5
tRNA

1

2

3

Next amino acid

Growing
polypeptide
chain

Ribosome

Anticodons

tRNA

tRNA

G

G

UA

AU

CG

CG

UA

C

C

D

E

Next amino acid

2

3

4

5

6

tRNA

tRNA

tRNA

A B

C

D

E

F

G

H

I

1

1

2

3

Figure 3.22 How secretory proteins enter the
endoplasmic reticulum. A protein destined for secretion
begins with a leader sequence that enables it to be inserted into
the cisterna (cavity) of the endoplasmic reticulum. Once it has
been inserted, the leader sequence is removed and carbohydrate
is added to the protein.

Ribosome

mRNA

Carbohydrate

Cisterna of
endoplasmic reticulum

Protein

Granular endoplasmic
reticulum

Cytoplasm

Leader
sequence
removed

Leader
sequence

Free ribosome

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